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The recombinant human RPSA protein is encoded by a recombinant DNA that was cloned into the expression vector and then transformed into the E.coli that supports the expression of the gene. The recombinant DNA was constructed by fusing the N-terminal 10xHis tag and C-terminal Myc tag gene to the gene fragment coding for the 2-295aa of the human RPSA protein. After purification, the product is the recombinant human RPSA protein. This recombinant RPSA protein was subjected to the SDS-PAGE determination. Its purity reaches over 90% evaluated by Bandscan software analysis combined with SAS-PAGE. This RPSA protein ran to the molecular weight of about 35-40 kDa under SDS-PAGE condition. It may have applications in cardiovascular research.RPSA protein is a ribosomal protein which encoded by RPSA gene in human. RPSA gene consists of seven exons, six of which correspond to the coding sequence. RPSA structure generally is divided in an N-domain (residues 1-209) and a C-domain (residues 210-295). The structure of the N-domain of RPSA is similar to those of prokaryotic RPS2. RPSA is originally discovered by methods of cellular biology. RPSA binds to proteins that are involved in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis.
The recombinant human RPSA protein is encoded by a recombinant DNA that was cloned into the expression vector and then transformed into the E.coli that supports the expression of the gene. The recombinant DNA was constructed by fusing the N-terminal 10xHis tag and C-terminal Myc tag gene to the gene fragment coding for the 2-295aa of the human RPSA protein. After purification, the product is the recombinant human RPSA protein. This recombinant RPSA protein was subjected to the SDS-PAGE determination. Its purity reaches over 90% evaluated by Bandscan software analysis combined with SAS-PAGE. This RPSA protein ran to the molecular weight of about 35-40 kDa under SDS-PAGE condition. It may have applications in cardiovascular research.RPSA protein is a ribosomal protein which encoded by RPSA gene in human. RPSA gene consists of seven exons, six of which correspond to the coding sequence. RPSA structure generally is divided in an N-domain (residues 1-209) and a C-domain (residues 210-295). The structure of the N-domain of RPSA is similar to those of prokaryotic RPS2. RPSA is originally discovered by methods of cellular biology. RPSA binds to proteins that are involved in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis.
| Cat.No | ACP02210 | Target Name | RPSA |
|---|---|---|---|
| Form | Liquid or Lyophilized powder | Expression System | E.coli |
| Expression Range | 2-295aa | Mol Weight | 37.7 kDa |
| Protein Length | Full Length of Mature Protein | Purity | Greater than 85% as determined by SDS-PAGE. |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P08865 |
|---|
Uniprot Id
P08865
Target Species
Human
Target Name
RPSA
Target Full Name
Small ribosomal subunit protein uS2
Target Function
Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Acts as a PPP1R16B-dependent substrate of PPP1CA.; (Microbial infection) Acts as a receptor for the Adeno-associated viruses 2,3,8 and 9.; (Microbial infection) Acts as a receptor for the Dengue virus.; (Microbial infection) Acts as a receptor for the Sindbis virus.; (Microbial infection) Acts as a receptor for the Venezuelan equine encephalitis virus.; (Microbial infection) Acts as a receptor for the pathogenic prion protein.; (Microbial infection) Acts as a receptor for bacteria.
Target Involvement
Asplenia, isolated congenital (ICAS)
Target Subcellular Location
Cell membrane. Cytoplasm. Nucleus.
Target Protein Families
Universal ribosomal protein uS2 family
Target Research Area
Cardiovascular
Target Synonyms
34/67 kDa laminin receptor; 37 kDa laminin receptor precursor; 37/67 kDa laminin receptor; 37LRP; 40S ribosomal protein SA; 67 kDa laminin receptor; 67LR; Colon carcinoma laminin binding protein; Colon carcinoma laminin-binding protein; LAMBR; Laminin receptor 1; Laminin-binding protein precursor p40; LAMR 1; LamR; LAMR1; LBP; LBP/p40; LRP; LRP/LR; Multidrug resistance associated protein MGr1 Ag; Multidrug resistance associated protein MGr1Ag; Multidrug resistance-associated protein MGr1-Ag; NEM/1CHD4; p40; Ribosomal Protein SA; rpsA; RSSA_HUMAN; SA
Target Background
Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Many of the effects of laminin are mediated through interactions with cell surface receptors. These receptors include members of the integrin family, as well as non-integrin laminin-binding proteins. This gene encodes a high-affinity, non-integrin family, laminin receptor 1. This receptor has been variously called 67 kD laminin receptor, 37 kD laminin receptor precursor (37LRP) and p40 ribosome-associated protein. The amino acid sequence of laminin receptor 1 is highly conserved through evolution, suggesting a key biological function. It has been observed that the level of the laminin receptor transcript is higher in colon carcinoma tissue and lung cancer cell line than their normal counterparts. Also, there is a correlation between the upregulation of this polypeptide in cancer cells and their invasive and metastatic phenotype. Multiple copies of this gene exist, however, most of them are pseudogenes thought to have arisen from retropositional events. Two alternatively spliced transcript variants encoding the same protein have been found for this gene.
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