2. Recombinant Proteins
  3. CAR-T Related Proteins CD Antigens Receptor Proteins
  4. B Cell CD Proteins Stem Cell CD Proteins Dendritic Cell CD Proteins Siglec
  5. Siglec-2/CD22
  6. Siglec-2/CD22 Protein, Rat (692a.a, HEK293, Fc)

Siglec-2/CD22 Protein, Rat (692a.a, HEK293, Fc)

Cat. No.: HY-P75431
Handling Instructions

The Siglec-2/CD22 protein mediates B cell interactions and may direct B cell localization within lymphoid tissues. It recognizes sialylated glycoproteins, especially α-2,6-linked sialic acid, and participates in cis-interactions at the cell surface. Siglec-2/CD22 Protein, Rat (692a.a, HEK293, Fc) is the recombinant rat-derived Siglec-2/CD22 protein, expressed by HEK293 , with C-hFc labeled tag. The total length of Siglec-2/CD22 Protein, Rat (692a.a, HEK293, Fc) is 692 a.a., with molecular weight of ~102 kDa.

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Description

The Siglec-2/CD22 protein mediates B cell interactions and may direct B cell localization within lymphoid tissues. It recognizes sialylated glycoproteins, especially α-2,6-linked sialic acid, and participates in cis-interactions at the cell surface. Siglec-2/CD22 Protein, Rat (692a.a, HEK293, Fc) is the recombinant rat-derived Siglec-2/CD22 protein, expressed by HEK293 , with C-hFc labeled tag. The total length of Siglec-2/CD22 Protein, Rat (692a.a, HEK293, Fc) is 692 a.a., with molecular weight of ~102 kDa.
Background

Siglec-2/CD22 Protein serves as a crucial mediator in B-cell interactions, potentially playing a role in the localization of B-cells within lymphoid tissues. Known for its ability to bind sialylated glycoproteins, including CD45, it exhibits a preference for alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. During the immune response, ligand-induced tyrosine phosphorylation suggests its involvement in the regulation of B-cell antigen receptor signaling. The protein's multifaceted role encompasses positive regulation through interaction with Src family tyrosine kinases, while concurrently acting as an inhibitory receptor by recruiting cytoplasmic phosphatases via their SH2 domains to block signal transduction through dephosphorylation of signaling molecules. Siglec-2/CD22 predominately exists as a monomer of isoform CD22-beta and can also form a heterodimer with a shorter isoform. Its intricate interactions with key molecules such as PTPN6/SHP-1, LYN, SYK, PIK3R1/PIK3R2, PLCG1, GRB2, INPP5D, and SHC1, especially upon phosphorylation, highlight its pivotal role in orchestrating complex signaling networks within B-cells. Further research is essential to unravel the precise molecular pathways and functional consequences of Siglec-2/CD22 in B-cell regulation and immune responses.
Species

Rat
Source

HEK293
Tag

C-hFc
Accession

D3ZD88 (M1-R692)
Gene ID
Molecular Construction
N-term
CD22 (M1-R692)
Accession # D3ZD88
hFc
C-term
Synonyms
B-cell receptor CD22; BL-CAM; CD22; T-cell surface antigen Leu-14
Molecular Weight

Approximately 102 kDa
Purity

Greater than 95% as determined by reducing SDS-PAGE
Endotoxin Level

<1 EU/μg, determined by LAL method.
Documentation
Handling Instructions (2659 KB)

Siglec-2/CD22 Protein, Rat (692a.a, HEK293, Fc) Related Classifications

Help & FAQs
  • Do most proteins show cross-species activity?

    Species cross-reactivity must be investigated individually for each product. Many human cytokines will produce a nice response in mouse cell lines, and many mouse proteins will show activity on human cells. Other proteins may have a lower specific activity when used in the opposite species.

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Specific Activity (Unit/mg) = 106 ÷ Biological Activity (ED50)
Unit/mg = 106 ÷ ng/mL

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