Recombinant Human Blood group Rh (RHCE) Protein (His-KSI)

Name: Recombinant Human Blood group Rh (RHCE) Protein (His-KSI)
Brand: Beta LifeScience
SKU: BLC-07853P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Blood group Rh (RHCE) Protein (His-KSI) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P18577
Target Symbol	RHCE
Synonyms	Rh polypeptide 1 (RhPI) (Rh30A) (RhIXB) (Rhesus C/E antigens)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-KSI
Target Protein Sequence	TSGLLTGLLLNLKIWKAPHVAKYFDDQVFWKFPHLAVGF
Expression Range	379-417aa
Protein Length	Partial
Mol. Weight	19.8 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane.
Subcellular Location	Membrane; Multi-pass membrane protein.
Protein Families	Ammonium transporter (TC 2.A.49) family, Rh subfamily
Database References	HGNC: 10008 OMIM: 111690 KEGG: hsa:6006 STRING: 9606.ENSP00000294413 UniGene: Hs.449968
Tissue Specificity	Restricted to tissues or cell lines expressing erythroid characters. Isoform 4g and isoform RhPI-Alpha are expressed in immature erythroblasts but not in mature erythroblasts.

Gene Functions References

Among the weak D phenotypes in Tunisia, no novel RHD allele was found and almost 90% were caused by alleles of the weak D Type 4 cluster, of which 88% represented the weak D Type 4.0 allele. Based on established RH haplotypes for variant RHD and RHCE alleles and the lack of adverse clinical reports, we recommend D+ transfusions for patients with weak D Type 4.0 in Tunisia. PMID: 29193104
study 94.9% of the partial D samples revealed altered RHCE variant alleles and 5.7% of the samples with altered RHD allele predicted partial c, partial e and the lack of the high prevalence hr(B) and hr(S) antigens. PMID: 27111588
sequence comparisons revealed high sequence similarity between Patr_RHbeta and Hosa_RHCE, while the chimpanzee Rh gene closest to Hosa_RHD was not Patr_RHalpha but rather Patr_RHgamma PMID: 26872772
The purpose of this study was to determine the diversity and frequency of RHD-CE genotypes, predicting partial antigens in patients with sickle cell disease and in African Brazilian donors in order to find, through the use of RH genotyping, more closely matched donors for sickle cell disease patients who are alloimmunised to Rh antigens. PMID: 27177398
The RHCE gene intron 4 of Han Chinese, Tibetans, and Mongols differs from the RHD gene intron 4 in the presence of a 652-bp fragment. PMID: 26579938
Six new RHCE alleles were identified, namely, RHCE*cE84A, RHCE*ce202G, RHCE*ce307T, RHCE*Ce377G, RHCE*ce697G,712G,733G,744C, and RHCE*Ce733G in individuals of diverse racial origin. PMID: 26435076
RHCE*cE94G encodes variable expression of c (RH4). PMID: 26286238
Rh antibodies in SCD patients with RH variants can be clinically significant and, therefore, matching patients based on RH variants should be considered. PMID: 24960646
Through molecular genotyping we also identified polymorphisms in RhCE, Kell, Duffy, Colton, Lutheran and Scianna loci in donors and patients. PMID: 25582271
An uneven distribution of RH variant alleles between Dogon and Fulani, in Mali. A high incidence of predicted partial-C phenotype encoded by RHCE*Ce-D(4)-ce was found in Fulani. PMID: 25857637
These data showed the presence of the (C)ce(s) haplotype at a low frequency (0.625%) compared to that among Africans in whom it is common. Nevertheless, the presence of RHD-CE-D(s) in Tunisians, even at a lower frequency PMID: 24333089
One allele was found to be the known allele RHCE*Ol.20.01(RHCE*ce733G) and the second was novel: RHCE*Ol.06.02(RHCE*ce254G,733G). PMID: 25695437
RHD*weak partial 4.0 is associated with an altered RHCE*ce(48C, 105T, 733G, 744C, 1025T) allele in the Tunisian population. PMID: 23742316
RHCE*ceMO was present in one in 50 African-American persons with an allele frequency of 0.01, is often linked to RHD*DAU0, and is potentially of clinical significance for transfusion. PMID: 23772606
In addition to hybrid alleles and nucleotide deletion, intronic mutations may be associated with the nonexpression of RhCE antigens. PMID: 23252593
A QMPSF-based method is reliable to individually quantify the exons of both RH genes, including hybrid D-CE genes in compound heterozygous samples. PMID: 23550903
Frequencies of aberrant RHD and RHCE alleles were similar, irrespective of location and ethnicity. PMID: 24033223
A novel RHCE*cE allele, RHCE*cE734C, was found in two probands whose red blood cells had weakened c expression and typed E- with conventional anti-E reagents. PMID: 22958092
RHD*DIVa and RHCE*ceTI almost always, but not invariably, travel together. This haplotype is found in people of African ancestry and the red blood cells can demonstrate aberrant reactivity with anti-C. RHCE*ceTI encodes partial c and e antigens. PMID: 22804620
Low-prevalence Rh antigen STEM (RH49) is encoded by two different RHCE*ce818T alleles that are often in cis to RHD*DOL. PMID: 22738288
The rare RHCE*ceBI allele appears to be in cis either with RHD*DOL1 or with RHD*DOL2 in people of African descent. PMID: 22690701
Two novel RHCE*ce 48C,733G,1006T alleles have been identified: RHD*186T and RHD*DIIIa150C. PMID: 23286557
A novel allele of RHCE, RHCE*cE 907delC, silences c and E and in the homozygous state resulting in a D- - phenotype and production of anti-Rh17. PMID: 21517889
Allele-specific oligonucleotide polymerase chain reaction for the determination of Rh C/c and Rh E/e antigens in thalassaemic patients. PMID: 21251469
Study identifies a novel allele, RHCE*ce 48C, 733G, 941C, 1006T which is predicted to encode 16Cys, 245Val, 314Ala, and 336CyS and was shown to encode c, V/VS, and an altered expression of e and hrB antigens. PMID: 20576012
RHCE*ceAR encodes a partial c (RH4) antigen. PMID: 20932075
The low prevalence Rh antigen, Be(a), is associated with a single nucleotide change in exon 5 of RHCE*ce; that of 662C>G. and This changes proline-221 of Rhce to arginine, which may impose a steric and/or charge-related effect on the protein. PMID: 19951310
JAL and JAHK antigens are expressed by Ce and ce and varients of RhCE protein PMID: 20233350
RHCE represents the ancestral RH position, while RHD is the duplicated gene PMID: 11902138
Molecular analysis of Hor+, Mol+ variants revealed a hybrid gene structure RHCe-D(5)-Ce, in which exon 5 of RHCE (RHCe allele) was replaced by exon 5 of RHD (the so-called RHCeVA allele). PMID: 12084172
strong selection might be working to maintain the RHCE/RHD antigen variation in the two-locus system PMID: 12857961
disruption of f (Rh6) by Arg229 deletion suggests that external loop 4 is a major structural element contributing to the expression of RHCE cis interacting antigenic products. PMID: 14996197
The single-point mutation T500A in exon 4 of the RHCE gene is a molecular basis of the rare Rhesus antigen Ew. PMID: 14996199
A high incidence of Trp16Cys in RHCE ce was seen in sickle cell disease. Many of these patients were heterozygous for VS antigen. cDNA analysis showed that the 2 mutations were on different alleles, weakening expression of the e antigen on RBCs. PMID: 15023184
Review. The genetic, structural, and immunologic features of RHCE are reviewed. PMID: 15373666
RhCE may not function directly in ammonia transport and may be evolving a new function in the RBC membrane. PMID: 16563829
Review. 3-D models of the subunit and oligomeric architecture are proposed, using hydrophobic cluster analysis. PMID: 16584906
Although the F223V substitution is regarded as the initial event in the evolution of the weak D Type 4 cluster, the current DFV allele probably evolved independently, as evident from different RHCE haplotypes PMID: 17900276
It is possible to examine fetal c allele of RHCE gene in the plasma of pregnant women with anti-c by means of a noninvasive method. PMID: 18382999
The nucleotide 340C>T change in RHCE exon 3 (predicted to encode 114Trp) of the RHCE*ce(S)(340) allele is associated with a JAL+ phenotype and the altered expression of the c, V and VS antigens. PMID: 19076333
Homology modeling of the JAL+ RhCE protein suggests that the Arg-->Trp change eliminates a critical loop-stabilizing H-bond between the side chain of Arg114 and the e-specific amino acid Ala226. PMID: 19170983
the previously described RhCeMA and ce(s)(340) alleles encode the JAL antigen. PMID: 19207167
RHcE(M167K) known as E variant I was the most frequent allele, found in 70 of 122 analyzed blood donors in the northwest of Germany. Among 13 referred samples, C typing problems predominated. PMID: 19453979
Single-amino-acid substitutions were the molecular basis for variant RhCE antigen expression in most samples of German blood donors and patients . PMID: 19453980

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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