Biotinylated Recombinant Human Blood group Rh (RHD) Protein (MBP&His-Avi)

Beta LifeScience SKU/CAT #: BLC-07546P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Biotinylated Recombinant Human Blood group Rh (RHD) Protein (MBP&His-Avi)

Beta LifeScience SKU/CAT #: BLC-07546P
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Product Overview

Description Biotinylated Recombinant Human Blood group Rh (RHD) Protein (MBP&His-Avi) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb Q02161
Target Symbol RHD
Synonyms (RHXIII)(Rh polypeptide 2)(RhPII)(Rhesus D antigen)(CD antigen CD240D)
Species Homo sapiens (Human)
Expression System E.coli
Tag N-MBP&C-6His-Avi
Expression Range 388-417aa
Protein Length Partial
Mol. Weight 51.4 kDa
Research Area Cardiovascular
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 Cell membrane; Multi-pass membrane protein.
Protein Families Ammonium transporter (TC 2.A.49) family, Rh subfamily
Database References
Tissue Specificity Restricted to tissues or cell lines expressing erythroid characters.

Gene Functions References

  1. 4 novel RHD alleles, each characterized by a single nucleotide substitution were identified. RHD*67T, RHD*173T, and RHD*579C give rise to a weak D phenotypical expression. Their corresponding amino acid changes are predicted to be located in the membrane-spanning or intracellular domains of the RhD protein. RHD*482G is the 4th substitution. PMID: 29052223
  2. Extensive studies show that the RHD*1227A is the most prevalent DEL allele in East Asian populations and may have confounded the initial molecular studies. PMID: 29214630
  3. The most prevalent DEL allele was RHD*DEL1 (c.1227G>A), which is proven to be immunogenic. A high frequency of RHD*Psi was detected in the donors with nondeleted RHD alleles (31%), far superior to the frequency of RHD variant alleles (15.5%). PMID: 29193119
  4. Absence of the whole RHD gene is common among RhD negative blood donors from Qingdao region, and there are rich genetic polymorphisms for this locus PMID: 29188626
  5. The RHD 1227G>A mutation contributes to the molecular basis of Del phenotype in the Taiwanese population. The point mutation results in aberrant frame shift or exon deletion transcripts and generates D protein with weak antigen presenting function. PMID: 26774048
  6. In this mixed Brazilian population, the most frequent weak D types were 1, 4, 3 and 2 (frequencies of 4.35%, 2.32%, 1.46% and 0.29%, respectively; total of 8.41%) and partial D was found in 2.90% of samples carrying the RHD gene. For samples with inconclusive RhD typing, 53.33% of them presented weak and partial RHD, and 43.75% had concomitantly more than one RHD variant PMID: 27184292
  7. sequence comparisons revealed high sequence similarity between Patr_RHbeta and Hosa_RHCE, while the chimpanzee Rh gene closest to Hosa_RHD was not Patr_RHa but rather Patr_RHy PMID: 26872772
  8. Six weak D types in the Russian Federation: the most common type 3 (49.2%) and type 1 (28.6%), type 2 (14.3), type 15 (4.8%), type 4.2 (DAR) (1.6%) and type 6 (1.6%). PMID: 27459619
  9. The frequency of RhD negative homozygosity in the Cypriot population was estimated to be 7.2%, while the frequencies of RHD hemizygosity and RhD positive homozygosity was calculated to be 39.2 and 53.6%, respectively. PMID: 27036548
  10. Occurrence of partial RhD alleles in the Tunisian population. PMID: 26482434
  11. Reduced expression of D antigen is caused not only by missense mutation of the RHD gene, but also by silent mutation that may affect splicing. PMID: 26340140
  12. Loss of heterozygosity of RhD gene on chromosome 1p in acute myeloid leukemia. PMID: 25495174
  13. The data indicate that partial DEL women appear at risk of alloimmunization to the D antigen. PMID: 26033335
  14. Weak D type 4.0 appears to be the most prevalent weak D in our population. However, all samples must be sequenced in order to determine the exact subtype of weak D type 4, since weak D type 4.2 has considerable clinical importance PMID: 25369614
  15. Paternal RHD zygosity determination in Tunisians: evaluation of three molecular tests. PMID: 24960665
  16. Serologic findings of RhD alleles in Egyptians and their clinical implications. PMID: 25219636
  17. Despite the enormous diversity of RHD alleles, first-line weak D genotyping was remarkably informative, allowing for rapid classification of most samples with conspicuous RhD phenotype in Flanders, Belgium. PMID: 25413499
  18. Splicing is altered in RHD*weak D Type 2 allele, a rare variant most commonly found in Caucasians; RHD including the full-length Exon 9 is transcribed in the presence of the c.1227G>A substitution frequently carried by Asians with DEL phenotype. PMID: 25808592
  19. Among all donors 89.00% and 10.86% were D-positive and D-negative, respectively, while 0.14% (n=55) of the donors were found to be weak D-positive. PMID: 24960662
  20. The frequency of D variants detected by IAT allele RHD(M295I) was 1:272 in D negative donors. Obviously, DEL phenotype is more common in some parts of European population than initially thought. PMID: 24556127
  21. New RHD variant alleles. PMID: 25179760
  22. Currently, it seems to be difficult to observe any new RHD alleles in the Han Chinese population. D prediction in this population is easier because popular alleles are dominant, accounting for about 99.80% of alleles in D-negative people. PMID: 24333088
  23. In Han Chinese people with weak D serotyping, 8 weak D and 4 partial D alleles were found. 3 new weak D alleles (RHD weak D 95A, 779G, and 670G) and one new partial D allele (RHD130-132 del TCT) were identified. PMID: 25070883
  24. DEL/weak D-associated RHD alleles were found in 2.17% of Australian D-, C+ and/or E+ blood donors. PMID: 24894016
  25. RHD alleles and D antigen density among serologically D- C+ Brazilian blood donors. PMID: 24267268
  26. In this study, D antigen density on the erythrocyte surface of DEL individuals carrying the RHD1227A allele was extremely low, there being only very few antigenic molecules per cell, but the D antigen epitopes were grossly complete. PMID: 24333082
  27. The prevalence of D-/RHD+ samples is higher than that observed in Europeans. More than 50% of the RHD alleles found were represented by RHDpsi and RHD-CE-D(s) showing the African contribution to the genetic pool of the admixed population analyzed. PMID: 24819281
  28. A method of genotyping has been developed in the laboratory. genotyping results of 200 pregnant women have been compared with RH1 phenotype at birth. PMID: 24559796
  29. We conclude that noninvasive fetal RHD genotyping from maternal blood provides accurate results and suggests its viability as a clinical tool for the management of RhD-negative pregnant women in an admixed population. PMID: 24615044
  30. Two molecular polymorphisms to detect the (C)ce(s) type 1 haplotype. PMID: 24333080
  31. This study analyzes the phenotype and frequency of RhD and tetanus toxoid specific memory B cells in limiting dilution culture. PMID: 24965774
  32. Data indicate that non-invasive prenatal testing of cell-free fetal DNA (cffDNA) in maternal plasma can predict the fetal RhD type in D negative pregnant women. PMID: 24204719
  33. DIV alleles arose from at least two independent evolutionary events. DIV Type 1.0 with DIVa phenotype belongs to the oldest extant human RHD alleles. DIV Type 2 to Type 5 with DIVb phenotype arose from more recent gene conversions. PMID: 23461862
  34. RHD*DARA and RHD*DAR2 are the same allele. Furthermore, the alleles RHD*DAR1.2 and RHD*DAR1.3 both exist; however, the silent mutation 957G>A (V319) showed no influence on the RhD phenotype. PMID: 23902153
  35. All novel weak D types expressed all tested D epitopes. PMID: 23550956
  36. Only 0.2% of D- Polish donors carry some fragments of the RHD gene; all of them were C or E+. Almost 60% of the detected RHD alleles may be potentially immunogenic when transfused to a D- recipient. PMID: 23634715
  37. This study is the first to describe weak D types caused by intronic variations near the splice sites in the RHD gene, which is supported by the genotyping results combined with serologic profiles and bioinformatics analysis. PMID: 23216299
  38. RHD variants were identified in 91.6% of the 430 studied samples. Two of the nine previously undescribed variants, c.335G>T and c.939G>A, were found to cause aberrant mRNA splicing by means of a splicing minigene assay. PMID: 23228153
  39. Hemizygous RHD subjects demonstrated significantly higher platelet increases and peak platelet counts than homozygous RHD subjects. PMID: 23712954
  40. The RHD*weak 4.3 allele with markedly reduced antigen D expression was shown to be associated with an altered RHCE gene formation leading to the expression of C(X) and VS. PMID: 22288371
  41. modulates the influence not only of latent toxoplasmosis, but also of at least two other potentially detrimental factors, age and smoking, on human behavior and physiology. PMID: 23209579
  42. 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. PMID: 22804620
  43. RHD*DOL2, like RHD*DOL1, encodes a partial D antigen and the low-prevalence antigen DAK. PMID: 22738288
  44. The use of cell-free fetal DNA in prenatal noninvasive early detection of fetal RhD status and gender by real-time PCR is highly sensitive and accurate as early as the 11th week of gestation for RhD status and the 7th week of gestation for fetal sex. PMID: 21488716
  45. This deletion appears to represent not only the first large deletion associated with weak D but also the weakest of weak D alleles so far reported. PMID: 22420867
  46. Characterization of novel RHD alleles. PMID: 22320258
  47. The RHD genotyping proved to be a necessary tool to characterise RHD alleles in donors phenotyped as D- or weak D to increase the transfusion safety in highly racial mixed population. PMID: 22211984
  48. RHD homozygotes had nearly twice as many D antigen sites as hemizygotes. Expression of c or E antigens was associated with increased RBC D antigen expression, but presence of C or e antigens reduced expression. PMID: 22121029
  49. Anti-D investigations in individuals expressing weak D Type 1 or weak D Type 2 PMID: 21658048
  50. Distribution of weak D types in the Croatian population. PMID: 21269342


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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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