产品详情
  • 产品名称:C-TypeLectinDomainFamily10,MemberA(CLEC10A)(AA61-292)(Active)protein(FcTag)

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  • 产品厂商:ACROBiosystems
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简单介绍:
C-TypeLectinDomainFamily10,MemberA(CLEC10A)(AA61-292)(Active)protein(FcTag)
详情介绍:
Characteristics This protein carries a human IgG1 Fc tag at the N-terminus. The protein has a calculated MW of 55.7 kDa. The protein migrates as 60-75 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Purity >92 % as determined by SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
Background C-type lectin domain family 10 member A (CLEC10A) is also known as C-type lectin superfamily member 14 (CLECSF14), Macrophage lectin 2, CD antigen CD301. CLEC10A / CD301 is a unique calcium-type (C-type) lectin, which expressed on Dendritic cells (DCs). CLEC10A / CD301 probable role in regulating adaptive and innate immune responses. CLEC10A / CD301 binds in a calcium-dependent manner to terminal galactose and N-acetylgalactosamine (GalNAc), linked to serine or threonine. There are two homologues in mice: MGL1 and MGL2 (CD301a and CD301b).
Molecular Weight 55.7 kDa
UniProt Q8IUN9
Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer 50 mM Tris, 100 mM Glycine, pH 7.5
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C), After reconstitution under sterile conditions for 3 months (-70 °C).
Supplier Images
SDS-PAGE (SDS) image for C-Type Lectin Domain Family 10, Member A (CLEC10A) (AA 61-292) (Active) protein (Fc Tag) (ABIN2180881) Human CLEC10A, Fc Tag on SDS-PAGE under reducing (R) condition. The gel was stained o...
Background publications Suzuki, Yamamoto, Toyoshima, Osawa, Irimura: "Molecular cloning and expression of cDNA encoding human macrophage C-type lectin. Its unique carbohydrate binding specificity for Tn antigen." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 156, Issue 1, pp. 128-35, 1996 (PubMed).