Recombinant Bovine Prolactin (PRL) Protein (His&Myc)

Name: Recombinant Bovine Prolactin (PRL) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-07255P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Bovine Prolactin (PRL) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P01239
Target Symbol	PRL
Species	Bos taurus (Bovine)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	TPVCPNGPGNCQVSLRDLFDRAVMVSHYIHDLSSEMFNEFDKRYAQGKGFITMALNSCHTSSLPTPEDKEQAQQTHHEVLMSLILGLLRSWNDPLYHLVTEVRGMKGAPDAILSRAIEIEEENKRLLEGMEMIFGQVIPGAKETEPYPVWSGLPSLQTKDEDARYSAFYNLLHCLRRDSSKIDTYLKLLNCRIIYNNNC
Expression Range	31-229aa
Protein Length	Full Length of Mature Protein
Mol. Weight	30.1 kDa
Research Area	Prolactin
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	Prolactin acts primarily on the mammary gland by promoting lactation.
Subcellular Location	Secreted.
Protein Families	Somatotropin/prolactin family
Database References	KEGG: bta:280901 STRING: 9913.ENSBTAP00000020313 UniGene: Bt.7197

Gene Functions References

Taken together, these results support novel functions of prolactin as a modulator of the innate immune response that do not involve the classical prolactin pathway. PMID: 26341952
The presence and localization of prolactin receptor are consistent with expression data reported for other species, and the presence of PIP and prolactin in seminal fluid is consistent with data generated in humans. PMID: 25533929
Functionally reciprocal mutations of the prolactin signaling pathway define hairy and slick cattle. PMID: 25519203
The single nucleotide polymorphism rs42646708 of cattle XKR4 was significantly associated with serum prolactin concentrations and explained 2.45% of the phenotypic variation. PMID: 24666329
Five mutations were identified in exonic region and eleven in associated intronic regions in PRL gene in 100 cattle from four Pakistani cattle breeds. PMID: 24065524
this study identifies a biochemical mechanism for the regulation of SCFAs on bovine GH and PRL gene transcription in dairy cow anterior pituitary cells PMID: 24177567
These data suggest that PRL protects brain endothelial cells against methamphetamine-induced toxicity PMID: 23988027
Bovine prolactin improved the expression of human transferrin through such a possible mechanism that bovine prolactin activated STAT5a transcription expression. PMID: 22829284
There was no significant difference between 1134 locus and milk performance traits of 5'-UTR of PRL gene PMID: 22207382
Staphylococcus aureus infection inhibits nuclear factor kappa B activation mediated by prolactin in bovine mammary epithelial cells. PMID: 21843629
Study of genetic variation in Yakutian cattle (Bos taurus L.) using the prolactin bPRL, growth hormone bGH, and transcription factor bPit-1 genes PMID: 20391788
This is the second study reporting single nucleotide polymorphisms in the 5'-regulatory region of PRL gene, which interfere with milk production traits. PMID: 19714484
evidence for a functional coupling between the PRL salt bridge and phosphorylation site indicates that either in vivo phosphorylation or specific mutations that destabilize the salt bridge impair biological activity. PMID: 12850287
determination of the effects of exposure to different lengths of daylight during the dry period on circulating PRL and PRL receptor mRNA expression in lymphocytes and mammary tissue during the transition to lactation PMID: 15591374
Expression of PRL and prolactin receptor (PRLR) mRNA is demonstrated for the first time in bovine corpus luteum throughout the luteal phase. PMID: 16435374
The A-->G transition at position -1043 abolishes the recognition site for Hsp92II restriction endonuclease. PMID: 17929163
Prolactin in ovarian follicular fluid stimulates endothelial cell proliferation. PMID: 19672107

FAQs

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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.