prolactin antagonist R129G Active Protein | PRL active protein

Ovine prolactin antagonist R129G

Cat. Num. AAA400061

• Purity: Greater than 99.0% as determined by:; (a) Gel filtration analysis.; (b) Analysis by reducing and non-reducing SDS-PAGE gel.
• Synonyms: prolactin antagonist R129G; Ovine prolactin antagonist R129G; Ovine prolactin antagonist G129R; PRL active protein

• Purity/Purification: Greater than 99.0% as determined by:; (a) Gel filtration analysis.; (b) Analysis by reducing and non-reducing SDS-PAGE gel.
• Form/Format: The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.

• Source: E.coli
• Physical Appearance: White lyophilized (freeze-dried) powder
• Solubility: It is recommended to reconstitute the lyophilized oPRL G129R in sterile water or 0.4% NaHCO₃ adjusted tp pH 8-9, not less than 100ug/ml, which can then be further diluted to other aqueous solutions, preferably in presence of carrier protein.
• Protein Content: Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.93 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.
• Dimers and Aggregates: The purified oPRL G129R (23K)or its truncared analogue consists of > 99% monomers as determined by gel-filtration chromatography.
• Endotoxin: Less than 0.1 ng/ug (IEU/ug) of oPRL G129R.
• Biological Activity: PLR's oPRL G129R is devoid of agonistic activity and capable of inhibiting biological activity of oPRL or other lactogenic hormones as evidenced by proliferation assay of Nb2 or other cells. The truncated form is more potent inhibitor.
• Amino Acid Sequence: The sequence of the first six N-terminal amino acids of the non-truncated form was determined and was found to be Ala-Thr-ProVal-Cys-Pro.
• Preparation and Storage: Lyophilized oPRL G129R although stable at room temperature for several weeks, should be stored desiccated below -18 degree C. Upon reconstitution at > 0.1 oPRL mg/ml and up to 4 mg/ml mM and filter sterilization oPRL can be stored at 4 degree C for several weeks.

Related Product Information for PRL active protein

Recombinant ovine prolactin, G129R muteln is one polypeptide chain containing 199 amino and an additional Ala at N-terminus acids'and having a molecular mass of ~23 kDa, was purified by proprietary chromatographic techniques (no published information). It is available in two forms: as full size protein and it its DES 9 aa truncated form from its N-terminus which has higher inhibitory activity.

Product Categories/Family for PRL active protein

Growth Hormones; prolactins; placental lactogens

NCBI and Uniprot Product Information

• NCBI GI #: 254675133
• NCBI GeneID: 5617
• NCBI Accession #: NP_001157030.1
• NCBI GenBank Nucleotide #: NM_001163558.2
• UniProt Accession #: P01236; Q15199; Q92996
• NCBI Official Full Name: prolactin
• NCBI Official Synonym Full Names: prolactin
• NCBI Official Symbol: PRL
• NCBI Protein Information: prolactin; decidual prolactin
• UniProt Protein Name: Prolactin
• UniProt Gene Name: PRL
• UniProt Synonym Gene Names: PRL
• UniProt Entry Name: PRL_HUMAN

NCBI Description

This gene encodes the anterior pituitary hormone prolactin. This secreted hormone is a growth regulator for many tissues, including cells of the immune system. It may also play a role in cell survival by suppressing apoptosis, and it is essential for lactation. Alternative splicing results in multiple transcript variants that encode the same protein. [provided by RefSeq, Aug 2011]

Uniprot Description

prolactin: Prolactin acts primarily on the mammary gland by promoting lactation. Belongs to the somatotropin/prolactin family.

Protein type: Secreted; Cytokine; Secreted, signal peptide; Motility/polarity/chemotaxis

Chromosomal Location of Human Ortholog: 6p22.3

Cellular Component: extracellular region

Molecular Function: protein binding; prolactin receptor binding; hormone activity

Biological Process: lactation; cell proliferation; cell surface receptor linked signal transduction; positive regulation of JAK-STAT cascade; regulation of multicellular organism growth; female pregnancy