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Catalog Number | orb257938 |
---|---|
Category | Proteins |
Description | Complement component 1 Q subcomponent-binding protein, mitochondrial (C1QBP), a member of the MAM33 family, is also known as ASF/SF2-associated protein p32, glycoprotein gC1qBP (C1qBP), mitochondrial matrix protein p32 and hyaluronan-binding protein 1, which is a homotrimer that contains three monomers forming a donut-shaped structure with an unusually asymmetric charge distribution on the surface. C1q associates with C1r and C1s in order to yield the first component of the serum complement system. C1QBP has also been identified as the p32 subunit of pre-mR splicing factor SF2, as well as a hyaluronic acid-binding protein. Furthermore, C1QBP has been shown to interact with Protein kinase D1, BAT2, PRKCD, PKC alpha and Protein kinase Mζ . |
Reactivity | Human |
Tag | C-6×His |
Form/Appearance | Powder |
Purity | 95% |
Conjugation | Unconjugated |
MW | 24.6 kDa |
Target | HABP1, C1QBP |
UniProt ID | Q07021 |
Protein Sequence | NP_001203.1 |
Source | Human HABP1, His Tag (orb257938) is expressed from E.coli cells. It contains AA His 75 - Gln 282 (Accession # Q07021-1). |
Expression System | E. coli |
Biological Origin | Human |
Expression Region | His 75 - Gln 282 |
Endotoxins | 1.0 EU per μg |
NCBI | NP_001203.1 |
Storage | -20°C |
Buffer/Preservatives | PBS, pH7.4 |
Alternative names | C1QBP,GC1QBP,HABP1,SF2P32,p33 Read more... |
Note | For research use only |
Application notes | This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 24.6 kDa. The protein migrates as 28-31 kDa under reducing (R) condition (SDS-PAGE). |
Expiration Date | 6 months from date of receipt. |
SDS-PAGE analysis of Human HABP1 protein
≥90% as determined by SDS-PAGE | |
This protein contains the human C1QBP(Leu74-Gln282) was fused with the C-terminal His Tag and expressed in E. coli. |
> 96%, determined by SDS-PAGE | |
This protein contains the mature form of human C1QBP (NP_0012031) (His 75-Gln 282) fused with two Met at N-terminus and a polyhistide tag at the C-terminus was expressed and purified and expressed from E. coli. |