14041 Results for: "small b30.2"

Supplier: Bioss

RFPL4B contains 1 B30.2/SPRY domain and 1 RING type zinc finger. The function of RFPL4B remains unknown.

Supplier: Bioss

RFPL4B contains 1 B30.2/SPRY domain and 1 RING type zinc finger. The function of RFPL4B remains unknown.

Supplier: Bioss

RFPL4B contains 1 B30.2/SPRY domain and 1 RING type zinc finger. The function of RFPL4B remains unknown.

Supplier: Prosci

TRIM48 belongs to the TRIM/RBCC family. It contains 1 B box-type zinc finger, 1 B30.2/SPRY domain and 1 RING-type zinc finger. The exact function of TRIM48 remains unknown.

Supplier: Prosci

RSPRY1 contains 1 B30.2/SPRY domain and 1 RING-type zinc finger. The exact function of RSPRY1 remains unknown.

Supplier: Prosci

RFPL4B contains 1 B30.2/SPRY domain and 1 RING-type zinc finger. The function of RFPL4B remains unknown.

Supplier: Bioss

RFPL4B contains 1 B30.2/SPRY domain and 1 RING type zinc finger. The function of RFPL4B remains unknown.

Supplier: Prosci

TRIM72 belongs to the TRIM/RBCC family. It contains 1 B box-type zinc finger and 1 B30.2/SPRY domain and 1 RING-type zinc finger. The function of TRIM72 remains unknown.

Supplier: Prosci

SPRY3 contains 1 B30.2/SPRY domain. Sprouty/Caveolin-1 interaction modulates signaling in a growth factor- and Sprouty isoform-specific manner. Spry 1, 2 and 3 expression was observed in placental tissue from all three trimestersl. The exact function of SPRY3 remains unknown.

Supplier: Bioss

RFPL4B contains 1 B30.2/SPRY domain and 1 RING type zinc finger. The function of RFPL4B remains unknown.

Supplier: Bioss

TRIM47 belongs to the TRIM/RBCC family. It contains one B box type zinc finger, one B30.2/SPRY domain and one RING type zinc finger. TRIM47 has low expression in most tissues; higher expression in kidney tubular cells and over expressed in astrocytoma tumor cells.

Supplier: Bioss

RFPL4B contains 1 B30.2/SPRY domain and 1 RING type zinc finger. The function of RFPL4B remains unknown.

Supplier: Bioss

RFPL4B contains 1 B30.2/SPRY domain and 1 RING type zinc finger. The function of RFPL4B remains unknown.

Supplier: Proteintech

TRIM67(Tripartite motif-containing protein 67) is also named as TNL and belongs to the belongs to the TRIM/RBCC family. The deduced protein contains an N-terminal RING finger domain, 2 B-boxes, a coiled-coil region, a COS box, an FN3 domain, and a B30.2 domain. TRIM67 shares 65% amino acid identity with TRIM9. This protein has 2 isoforms produced by alternative splicing.

Supplier: Bioss

RFPL4B contains 1 B30.2/SPRY domain and 1 RING type zinc finger. The function of RFPL4B remains unknown.

Supplier: Prosci

Tripartite motif-containing Motif 5 is a protein that in humans is encoded by the TRIM5 gene.It is a 493 amino acids protein that belongs to the TRIM/RBCC family.It contains 1 B box-type zinc finger, 1 B30.2/SPRY domain and 1 RING-type zinc finger. TRIM5 present in the cytoplasm recognizes motifs within the capsid proteins and interferes with the uncoating process, therefore preventing successful reverse transcription and transport to the nucleus of the viral genome. The exact mechanism of action has not been shown conclusively, but capsid protein from restricted viruses is removed by proteasome-dependent degradation

Supplier: Prosci

SPRYD5 Antibody: The SPRY domain-containing protein 5 (SPRYD5) is a member of a family of proteins whose sole common characteristic is the presence of a SPRY domain. SPRY domains are structural domains that were first described in the fungal Dictyostelium discoideum tyrosine kinase spore lysis A. In most systems SPRY domains provide binding sites for regulatory proteins or intramolecular binding sites that maintain the structural integrity of a protein. SPRYD5 belongs to the TRIM/RBCC family and contains one B box-type zinc finger, one B30.2/SPRY domain and one RING-type zinc finger. Little is known of the function of the SPRYD5 protein.

Supplier: Bioss

RFPL4B contains 1 B30.2/SPRY domain and 1 RING type zinc finger. The function of RFPL4B remains unknown.

Supplier: Bioss

RFPL4B contains 1 B30.2/SPRY domain and 1 RING type zinc finger. The function of RFPL4B remains unknown.

Supplier: Bioss

RFPL4B contains 1 B30.2/SPRY domain and 1 RING type zinc finger. The function of RFPL4B remains unknown.

Supplier: Prosci

RFPL2 contains 1 B30.2/SPRY domain and 1 RING-type zinc finger. The human RFPL2 gene has a role in neocortex development.

Supplier: Prosci

TRIM43 belongs to the TRIM/RBCC family. It contains 1 B box-type zinc finger, 1 B30.2/SPRY domain and 1 RING-type zinc finger. The exact function of TRIM43 remains unknown.

Supplier: Prosci

BTNL8 is a single-pass type I membrane protein. It belongs to the immunoglobulin superfamily, BTN/MOG family. BTNL8 contains 1 B30.2/SPRY domain and 1 Ig-like V-type domain. The exact function of BTNL8 remains unknown.

Supplier: Brady Worldwide

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Supplier: Prosci

Human Erythroid Membrane-Associated Protein (ERMAP) is a cell surface transmembrane protein that belongs to the immunoglobulin superfamily. It is hghly expressed in bone marrow and to a lower extent in leukocytes, thymus, lymph node and spleen. ERMAP contains 1 B30.2/SPRY domain and 1 Ig-like V-type (immunoglobulin-like) domain. It may serve as an erythroid cell receptor, possibly as a mediator of cell adhesion. ERMAP is responsible for the Scianna/Radin blood group system. Two transcript variants encoding the same protein have been found for this gene ERMAP.

Supplier: Bioss

The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM50 (tripartite motif containing 50), also known as TRIM50A or E3 ubiquitin-protein ligase TRIM50, is a 487 amino acid cytoplasmic protein that functions as an E3 ubiquitin-protein ligase. Containing one RING-type zinc finger, a B30.2/SPRY domain and a single B box-type zinc finger, TRIM50 belongs to the TRIM/RBCC family and undergoes post-translational auto-ubiquitination. TRIM50 exists as two alternatively spliced isoforms, designated TRIM50 alpha and TRIM50 beta, and has the ability to form dimers and trimers. The gene encoding TRIM50 maps to human chromosome 7, which houses over 1,000 genes, comprises nearly 5% of the human genome and has been linked to Osteogenesis imperfecta, Pendred syndrome, Lissencephaly, Citrullinemia and Shwachman-Diamond syndrome.

Supplier: Bioss

Midline-1 (Tripartite motif-containing protein 18, Putative transcription factor XPRF, RING finger protein 59) is a 667 amino acid protein encoded by the human gene MID1. Midline-1 belongs to the TRIM/RBCC family and contains two B box-type zinc fingers, one B30.2/SPRY domain, one COS domain, one fibronectin type-III domain and one RING-type zinc finger. Midline-1 is believed to have E3 ubiquitin ligase activity which targets the catalytic subunit of protein phosphatase 2 for degradation. It is a cytoplasmic protein found as a homodimer or heterodimer with Midline-2. It also interacts with IGBP1 (Lymphocyte signaling protein A4). Defects in MID1 are the cause of Opitz syndrome type I (OS-I). OS-I is an X-linked recessive disorder characterized by hypertelorism, genital-urinary defects such as hypospadias in males and splayed labia in females, lip-palate-laryngotracheal clefts, imperforate anus, developmental delay and congenital heart defects. OS-I mutations produce proteins with a decreased affinity for microtubules.

Supplier: Bioss

Midline-1 (Tripartite motif-containing protein 18, Putative transcription factor XPRF, RING finger protein 59) is a 667 amino acid protein encoded by the human gene MID1. Midline-1 belongs to the TRIM/RBCC family and contains two B box-type zinc fingers, one B30.2/SPRY domain, one COS domain, one fibronectin type-III domain and one RING-type zinc finger. Midline-1 is believed to have E3 ubiquitin ligase activity which targets the catalytic subunit of protein phosphatase 2 for degradation. It is a cytoplasmic protein found as a homodimer or heterodimer with Midline-2. It also interacts with IGBP1 (Lymphocyte signaling protein A4). Defects in MID1 are the cause of Opitz syndrome type I (OS-I). OS-I is an X-linked recessive disorder characterized by hypertelorism, genital-urinary defects such as hypospadias in males and splayed labia in females, lip-palate-laryngotracheal clefts, imperforate anus, developmental delay and congenital heart defects. OS-I mutations produce proteins with a decreased affinity for microtubules.

Supplier: Bioss

Midline-1 (Tripartite motif-containing protein 18, Putative transcription factor XPRF, RING finger protein 59) is a 667 amino acid protein encoded by the human gene MID1. Midline-1 belongs to the TRIM/RBCC family and contains two B box-type zinc fingers, one B30.2/SPRY domain, one COS domain, one fibronectin type-III domain and one RING-type zinc finger. Midline-1 is believed to have E3 ubiquitin ligase activity which targets the catalytic subunit of protein phosphatase 2 for degradation. It is a cytoplasmic protein found as a homodimer or heterodimer with Midline-2. It also interacts with IGBP1 (Lymphocyte signaling protein A4). Defects in MID1 are the cause of Opitz syndrome type I (OS-I). OS-I is an X-linked recessive disorder characterized by hypertelorism, genital-urinary defects such as hypospadias in males and splayed labia in females, lip-palate-laryngotracheal clefts, imperforate anus, developmental delay and congenital heart defects. OS-I mutations produce proteins with a decreased affinity for microtubules.

Supplier: Prosci

TRIM5 gamma Antibody: TRIM5 is a member of a broad family of otherwise unrelated proteins defined by the presence of a tripartite motif containing a RING domain, a B-box type 1, and a B-box type 2, followed by a coiled-coil region. TRIM5 has five alternately spliced isoforms, the longest of which is the alpha variant which also contains a carboxy-terminal B30.2 (SPRY) domain. While a function has not yet been assigned to TRIM5gamma, it is known that expression of TRIM5alpha variants from humans, rhesus monkeys, and African green monkeys enable resistance to infection by various retroviruses including HIV-1, albeit at differing efficiencies. Furthermore, the TRIM5delta isoform appears to serve as a scaffold for the assembly of endogenous BTBD1 and BTBD2 proteins and also exhibits autoubiquitination activity in a RING finger- and UbcH5B-dependent manner.