Search: 1000 results found for "Placental Growth Factor"

Description:

WNT Inhibitory Factor 1 Human Recombinant

WIF1, WIF-1, Wnt inhibitory factor 1.

Product # :

PRO-684

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Description

WIF1 Human is a single, glycosylated polypeptide chain containing 360 amino acids (29-379 a.a.) and having a molecular mass of 39.5 kDaWIF1 is fused to 6 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The WIF1 protein solution contains 1X PBS pH 7.4, 20% glycerol, 1mM DTT and 0.1mM PMSF.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
WIF1 binds to wnt proteins and inhibits their activities. WIF1 plays a role in mesoderm segmentation. WNT proteins are extracellular signaling molecules that take part in the control of embryonic development & cancer. WIF1 protein contains a WNT inhibitory factor (WIF) domain and 5 epidermal growth factor (EGF)-like domains. WIF1 takes part in mesoderm segmentation. WIF1 protein is found to be present in fish, amphibia and mammals. WIF1 is a recurrent target in human salivary gland oncogenesis. Downregulation of WIF1 takes part in the development and progression of pleomorphic adenomas. WIF1 is a tumor suppressor, specifically in nonfunctioning pituitary tumors.
Synonyms
WIF1, WIF-1, Wnt inhibitory factor 1.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADLGPPQEES LYLWIDAHQA RVLIGFEEDI LIVSEGKMAP FTHDFRKAQQ RMPAIPVNIH SMNFTWQAAG QAEYFYEFLS LRSLDKGIMA DPTVNVPLLG TVPHKASVVQ VGFPCLGKQD GVAAFEVDVI VMNSEGNTIL QTPQNAIFFK TCQQAECPGG CRNGGFCNER RICECPDGFH GPHCEKALCT PRCMNGGLCV TPGFCICPPG FYGVNCDKAN CSTTCFNGGT CFYPGKCICP PGLEGEQCEI SKCPQPCRNG GKCIGKSKCK CSKGYQGDLC SKPVCEPGCG AHGTCHEPNK CQCQEGWHGR HCNKRYEASL IHALRPAGAQ LRQHTPSLKK AEERRDPPES NYIWHHHHHH

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Prolactin Rabbit Soluble Receptor Recombinant

PRL-R.

Product # :

CYT-268

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Description

Prolactin Receptor Rabbit Extra Celleular Domain Recombinant ?produced in E.Coli is a non-glycosylated, Polypeptide chain containing 207 amino acids and having a molecular mass of 23972 Dalton. The Prolactin Receptor is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

Purity

Greater than 97.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Activity is determined by the dose-dependant inhibition of Prolactin-stimuled proliferation of Nb2 cells and by high affinity binding of oPLR and other lactogenic hormones. Refs:
1) Bignon et al. (1994) JBC 269; 3318-24
2) Gertler et al. (1996) JBC 271; 24482-91.

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Introduction
Prolactin is a pituitary hormone involved in the stimulation of milk production, salt and water regulation, growth, development and reproduction. The initial step in its action is the binding to a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. The function of the prolactin receptor is mediated, at least in part, by two families of signaling molecules: Janus kinases and signal transducers and activators of transcription. Prolactin (PRL) is a hormone involved in a variety of important functions including ion transport and osmoregulation, stimulation of milk, protein synthesis as well as the regulation of numerous reproductive functions. PRL exerts its influence on different cell types through a signal transduction pathway which begins with the binding of the hormone to a transmembrane PRL receptor. Immunoreactive PRL receptor, a member of the cytokine receptor family, varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL receptor consists of at least three separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.
Synonyms
PRL-R.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PRL-R although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prolactin Receptor should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized PRL-R in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Lys-Pro-Phe-Ile.
Protein content
UV spectroscopy at 280 nm using the absorbency value of 2.63 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENEcomputer analysis program of protein sequences (IntelliGenetics).

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Osteopontin 1 Mouse Recombinant

Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1

Product # :

CYT-1201

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Description

SPP1 Mouse Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 287 amino acids (17-294 a.a) and having a molecular mass of 31.8kDa.SPP1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The SPP1 solution (0.25mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured by the ability of the immobilized protein to support the adhesion of HEK293 HEK cells when the cells are added to mouse SPP1 coated plates. The ED50 range is ≤ 1.5 ug/ml.

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Introduction
Osteopontin is a glycoprotein that was first identified in osteoblasts and is involved in bone remodeling, immune functions in fibroblasts, macrophages, and lymphocytes during inflammation and wound healing. SPP1 binds tightly to hydroxyapatite. SPP1 forms an integral part of the mineralized matrix. SPP1 is vital to cell-matrix interaction. Secreted Phosphoprotein-1 protects against cardiac ischemia-reperfusion injury via late preconditioning. Expression of both Ostepontin and CD44 in hepatocellular carcinoma is linked with advanced tumor stage and contributes to prognosis information. SPP1 is the most over-expressed gene in intrahepatic cholangiocarcinoma. Secreted Phosphoprotein-1 overexpression is related with interstitial lung diseases.
Synonyms
Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
DGSLPVKVTD SGSSEEKLYS LHPDPIATWL VPDPSQKQNL LAPQNAVSSE EKDDFKQETL PSNSNESHDH MDDDDDDDDD DGDHAESEDS VDSDESDESH HSDESDETVT ASTQADTFTP IVPTVDVPNG RGDSLAYGLR SKSRSFQVSD EQYPDATDED LTSHMKSGES KESLDVIPVA QLLSMPSDQD NNGKGSHESS QLDEPSLETH RLEHSKESQE SADQSDVIDS QASSKASLEH QSHKFHSHKD KLVLDPKSKE DDRYLKFRIS HELESSSSEV NHHHHHH

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Nephroblastoma Overexpressed (260-357 a.a.) Human Recombinant

Igfbp9, igfbp-9.

Product # :

CYT-1234

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Description

The IGFBP9 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The IGFBP9 His-Tagged Fusion Protein, produced in E. coli, is a 18kDa protein containing 98 amino acid residues of the IGFBP9 Human, 260-357 amino acids.

Source

Escherichia Coli.

Formulation

Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Synonyms
Igfbp9, igfbp-9.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized IGFBP9 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Background
Nephroblastoma Overexpressed (NOV) is a part of the CCN (CTGF/CYR61/NOV) family which takes an important part in tissue repair and cellular signaling, differentiation and growth. NOV takes part in angiogenesis, extracellular matrix remodeling and cellular adhesion. NOV is also involved in reducing tumorgenicity and proliferation of certain cancer cell lines. NOV interacts with numerous proteins and participates in both internal and external cell signaling. NOV is expressed in tumors, including Wilm’s tumor and most nephroblastomas and is also exerts proangiogenic activities.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Glia Maturation Factor Beta, Mouse Anti Human

Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF.

Product # :

ANT-680

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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
Glia Maturation Factor-Beta (GMF-Beta) is a 17 kDa protein nerve gorwth factor identified as a growth and differentiation factor in the vertebrate brain.
Glia Maturation Factor-Beta stimulates differentiation of normal neurons as well as glial cells. GMFB inhibits the proliferation of the N-18 neuroblastoma line and the C6 glioma line while promoting their phenotypic expression.
GMF-beta inhances the phenotypic expression of glia & neurons thus inhibits the proliferation of their respective tumors when added to cell culture. Although astrocytes produce GMF-b and stores it inside the cells, they don’t secrete the GMF-B into the cultured medium. Cell- surface GMFb acts on the target cells at close range when cells are in direct contact. GMF-Beta is produced by thymic epithelial cells and plays an important role in T cell development in favor of CD4+ T cells.
GMF-Beta is a brain-specific protein which belongs to the actin-binding proteins (ADF) family. GMF-beta appears to play a role in the differentiation, maintenance, and regeneration of the nervous system. It also supports the progression of certain auto-immune diseases, possibly through its ability to induce the production and secretion of various pro-inflammatory cytokines.
Synonyms
Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human GMFB mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human GMFB amino acids 1-142 purified from E. coli.
Ig Subclass
Mouse IgG2a heavy chain and Kappa light chain.
Clone
PAT44D8AT.
Applications
GMFB antibody has been tested by ELISA, Western blot and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
GMFB antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Epigen Human Recombinant, His Tag

EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.

Product # :

CYT-794

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Description

EPGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 111 amino acids (23-110 a.a) and having a molecular mass of 12.1kDa.EPGN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

EPGN protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
EPGN is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. EPGN is produced in numerous tissues, including the testis, liver, heart and in certain tumor cells. EPGN is mitogenic for fibroblasts and epithelial cells. Human EPGN is originally synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence.
Synonyms
EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE K
Background
What is the molecular weight/Mw of EPIGEN Protein?
EPIGEN Protein has a total Mw of 12.1kDa.

What is the source or expression system of EPIGEN Protein?
Escherichia Coli.

What is the Purity of EPIGEN Protein?
EPIGEN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of EPIGEN Protein?
The biological functionality of EPIGEN Protein will be determined in the future.

What is the amino acid sequence of EPIGEN Protein?
MGSSHHHHHH SSGLVPRGSH MGSAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE K

What applications can EPIGEN Protein be used in?
EPIGEN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EPIGEN Protein?
The endotoxin level is minimal, EPIGEN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Oncostatin-M Human Recombinant (195 a.a.)

OSM, MGC20461, Oncostatin M.

Product # :

CYT-735

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Description

Oncostatin-M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids and having a molecular mass of 22kDa. The OSM is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing 1xPBS pH-7.4.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of the proliferation of human TF-1 cells is < 0.2ng/ml, corresponding to a specific activity of > 5.0x10⁶ units/mg.

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Introduction
Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.
Synonyms
OSM, MGC20461, Oncostatin M.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Oncostatin M although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Oncostatin M in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AAIGSCSKEY RVLLGQLQKQ TDLMQDTSRL LDPYIRIQGL DVPKLREHCR ERPGAFPSEE TLRGLGRRGF LQTLNATLGC VLHRLADLEQ RLPKAQDLER SGLNIEDLEK LQMARPNILG LRNNIYCMAQ LLDNSDTAEP TKAGRGASQP PTPTPASDAF QRKLEGCRFL HGYHRFMHSV GRVFSKWGES PNRSR.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Prolactin Soluble Receptor Rat Recombinant

PRL-R, Prolactin receptor, Lactogen receptor, Prlr.

Product # :

CYT-533

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Description

Prolactin Receptor Rat Extra Celleular Domain Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 206 amino acids and having a molecular mass of 24120 Dalton. The Prolactin Receptor is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

Purity

Greater than 97.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Activity is determined by the dose-dependant inhibition of Prolactin-stimuled proliferation of Nb2 cells and by high affinity binding of oPLR and other lactogenic hormones.

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Introduction
Prolactin is a pituitary hormone involved in the stimulation of milk production, salt and water regulation, growth, development and reproduction. The initial step in its action is the binding to a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. The function of the prolactin receptor is mediated, at least in part, by two families of signaling molecules: Janus kinases and signal transducers and activators of transcription. Prolactin (PRL) is a hormone involved in a variety of important functions including ion transport and osmoregulation, stimulation of milk, protein synthesis as well as the regulation of numerous reproductive functions. PRL exerts its influence on different cell types through a signal transduction pathway which begins with the binding of the hormone to a transmembrane PRL receptor. Immunoreactive PRL receptor, a member of the cytokine receptor family, varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL receptor consists of at least three separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.
Synonyms
PRL-R, Prolactin receptor, Lactogen receptor, Prlr.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PRL-R although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prolactin Receptor should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized PRL-R in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Lys-Pro-Glu-Ile.
Protein content
Protein quantitation was carried out by two independent methods 1. UV spectroscopy at 280 nm using the absorbency value of 2.48 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).2. Analysis by RP-HPLC, using a standard solution of PRLr-ECD as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Galectin-9 Mouse Recombinant

Galectin-9, Gal-9, Lgals9, Lgals5, LGALS35, AA407335, AI194909, AI265545.

Product # :

CYT-550

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SDS-PAGE

Description

LGALS9 mouse Recombinant produced E. coli is a single polypeptide chain containing 345 amino acids (1-322) and having a molecular mass of 38kDa.LGALS9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The LGALS9 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
LGLAS9 binds galactosides and has high affinity for the Forssman pentasaccharide. LGLAS9 participates in thymocyte-epithelial interactions relevant to the biology of the thymus and Inhibits cell proliferation. LGLAS9 is a ligand for HAVCR2/TIM3. LGLAS9 Induces T-helper type 1 lymphocyte (Th1) death. LGLAS9 performs as an eosinophil chemoattractant LGLAS9 is an S-type lectin which is over-expressed in Hodgkin's disease tissue and takes part in the interaction between the H&RS cells with their surrounding cells.
Synonyms
Galectin-9, Gal-9, Lgals9, Lgals5, LGALS35, AA407335, AI194909, AI265545.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMALFSAQ SPYINPIIPF TGPIQGGLQE GLQVTLQGTT KSFAQRFVVN FQNSFNGNDI AFHFNPRFEE GGYVVCNTKQ NGQWGPEERK MQMPFQKGMP FELCFLVQRS EFKVMVNKKF FVQYQHRVPY HLVDTIAVSG CLKLSFITFQ TQNFRPAHQA PMAQTTIHMV HSTPGQMFST PGIPPVVYPT PAYTIPFYTP IPNGLYPSKS IMISGNVLPD ATRFHINLRC GGDIAFHLNP RFNENAVVRN TQINNSWGQE ERSLLGRMPF SRGQSFSVWI ICEGHCFKVA VNGQHMCEYY HRLKNLQDIN TLEVAGDIQL THVQT.
Background
What is the molecular weight/Mw of LGALS9 MOUSE Protein?
LGALS9 MOUSE Protein has a total Mw of 38kDa.

What is the source or expression system of LGALS9 MOUSE Protein?
Escherichia Coli.

What is the Purity of LGALS9 MOUSE Protein?
LGALS9 MOUSE Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of LGALS9 MOUSE Protein?
The biological functionality of LGALS9 MOUSE Protein will be determined in the future.

What is the amino acid sequence of LGALS9 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMALFSAQ SPYINPIIPF TGPIQGGLQE GLQVTLQGTT KSFAQRFVVN FQNSFNGNDI AFHFNPRFEE GGYVVCNTKQ NGQWGPEERK MQMPFQKGMP FELCFLVQRS EFKVMVNKKF FVQYQHRVPY HLVDTIAVSG CLKLSFITFQ TQNFRPAHQA PMAQTTIHMV HSTPGQMFST PGIPPVVYPT PAYTIPFYTP IPNGLYPSKS IMISGNVLPD ATRFHINLRC GGDIAFHLNP RFNENAVVRN TQINNSWGQE ERSLLGRMPF SRGQSFSVWI ICEGHCFKVA VNGQHMCEYY HRLKNLQDIN TLEVAGDIQL THVQT.
What applications can LGALS9 MOUSE Protein be used in?
LGALS9 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for LGALS9 MOUSE Protein?
The endotoxin level is minimal, LGALS9 MOUSE Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Growth Hormone Rainbow Trout (Oncorhynchus mykiss) Recombinant

GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

Product # :

CYT-1010

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Description

Somatotropin Rainbow Trout (Oncorhynchus mykiss) Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids with an additional Ala at the N-terminus and having a molecular mass of 21, 535 Dalton. The Rainbow Trout (Oncorhynchus mykiss) Growth-Hormone Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.5% NaHCO3. Adjusted to pH-8.

Purity

Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Somatotropin Rainbow Trout (Oncorhynchus mykiss) Recombinant is biologically active in PDF-P1 3B9 cells stable transfected with rabbit GH receptors, though its activity is about 10 fold lower than that of human GH.

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Introduction
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
Synonyms
GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Growth-Hormone Rainbow Trout (Oncorhynchus mykiss) although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 for up to 4 weeks. For long term storage and more diluted solutions it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Growth-Hormone Rainbow Trout (Oncorhynchus mykiss) in 0.4% NaHCO3 or water adjusted to pH 8-9, not less than 100µg/ml and not more than 3mg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.
Amino Acid Sequence
AIENQRLFNIAVSRVQHLHLLAQKMFNDFDGTLLPDERRQLNKIFLLDFCNSDSIVSPVD
KHETQKSSVLKLLHISFRLIESWEYPSQTLIISNSLMVRNANQISEKLSDLKVGINLLIT
GSQDGVLSLDDNDSQQLPPYGNYYQNLGGDGNVRRNYELLACFKKDMHKVETYLTVAKCR
KSLEANCTL.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Growth Arrest and DNA-Damage-Inducible Gamma Interacting Protein 1 Human Recombinant

Growth arrest and DNA-damage-inducible gamma interacting protein 1, PRG6, CRIF1, PLINP-1, KBBP2, Plinp1, Papillomavirus L2-interacting nuclear protein 1, CKII beta-associating protein, CR6-interacting factor 1, p53-responsive gene 6 protein, CKII beta binding protein 2, growth arrest and DNA damage-inducible proteins-interacting protein 1, papillomavirus L2 interacting nuclear protein 1, PLINP1.

Product # :

PRO-972

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Description

GADD45GIP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 196 amino acids (48-222) and having a molecular mass of 22.6 kDa.GADD45GIP1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The GADD45GIP1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.2M NaCl and 40% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
GADD45GIP1 is a nuclear protein which takes part in apoptosis control. GADD45GIP1 is expressed in several tissues, such as heart, thyroid, trachea, kidney, ovary, pancreas, testis and stomach and acts as a negative regulator of G1 to S phase cell cycle production by collaborating with GADD45 proteins to inhibit the activity of cyclin-dependent kinases.
Synonyms
Growth arrest and DNA-damage-inducible gamma interacting protein 1, PRG6, CRIF1, PLINP-1, KBBP2, Plinp1, Papillomavirus L2-interacting nuclear protein 1, CKII beta-associating protein, CR6-interacting factor 1, p53-responsive gene 6 protein, CKII beta binding protein 2, growth arrest and DNA damage-inducible proteins-interacting protein 1, papillomavirus L2 interacting nuclear protein 1, PLINP1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPRWQLGPRY AAKQFARYGA ASGVVPGSLW PSPEQLRELE AEEREWYPSL ATMQESLRVK QLAEEQKRRE REQHIAECMA KMPQMIVNWQ QQQRENWEKA QADKERRARL QAEAQELLGY QVDPRSARFQ ELLQDLEKKE RKRLKEEKQK RKKEARAAAL AAAVAQDPAA SGAPSS

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

POU Class 5 Homeobox 1 Human Recombinant

POU domain class 5 transcription factor 1, Octamer-binding protein 3, Oct-3, Octamer-binding protein 4, Oct-4, Octamer-binding transcription factor 3, OTF-3, POU5F1, OCT3, OCT4, OTF3, OTF4, MGC22487.

Product # :

PRO-088

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Description

POU5F1 Human Recombinant produced in E. coli is a single polypeptide chain containing 285 amino acids (1-265) and having a molecular mass of 32.2 kDa.POU5F1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The POU5F1 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
POU5F1 is a homeodomain transcription factor of the POU family, expressed in embryonic stem (ES) cells and embryonic carcinoma (EC) cells.POU5F1 is significantly involved in the signaling pathway for maintaining self-renewal and pluripotency of ES cells. POU5F1 has 2 distinct DNA binding domains which independently bind half-sites of the canonical octamer motif. This flexibility allows POU5F1 to bind with distinct DNA motifs by forming heterodimers with other transcription factors or by forming homodimers in several conformations. Human POU5F1 contains a 75aa POU specific (POUS) domain and a 60aa POU-Homeo-(POUH) domain connected by a linker region. The Human POU5F1 specifically interacts with Octamer motif ATGCAAAT. In addition, 2 proline-rich domains in the N-terminal and C-terminal regions are vital for POU5F1 transactivation. POU5F1 regulates a number of target genes and has been shown to work jointly with other transcription factors including Sox2 as well as Nanog to sustain stem cell potency and self-renewal.
Synonyms
POU domain class 5 transcription factor 1, Octamer-binding protein 3, Oct-3, Octamer-binding protein 4, Oct-4, Octamer-binding transcription factor 3, OTF-3, POU5F1, OCT3, OCT4, OTF3, OTF4, MGC22487.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MHFYRLFLGA TRRFLNPEWK GEIDNWCVYV LTSLLPFKIQ SQDIKALQKE LEQFAKLLKQ KRITLGYTQA DVGLTLGVLF GKVFSQTTIC RFEALQLSFK NMCKLRPLLQ KWVEEADNNE NLQEICKAET LVQARKRKRT SIENRVRGNL ENLFLQCPKP TLQQISHIAQ QLGLEKDVVR VWFCNRRQKG KRSSSDYAQR EDFEAAGSPF SGGPVSFPLA PGPHFGTPGY GSPHFTALYS SVPFPEGEAF PPVSVTTLGS PMHSN.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

TNF Ligand Receptor Superfamily Member 12A Human Recombinant

Tumor necrosis factor receptor superfamily member 12A, FN14, CD266 antigen, TweakR, tweak-receptor, Fibroblast growth factor-inducible immediate-early response protein 14, FGF-inducible 14, type I transmembrane protein Fn14.

Product # :

CYT-043

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Description

TNFRSF12A Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 5.6 KDa.The TNFRSF12A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The TNFRSF12A biological activity is determined by its ability to inhibit TWEAK-induced weak cell death of HT29 cells. The expected ED50 for this effect is 1.0-5.0ug/ml in the presence of 1ug/ml rhTWEAK.

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Introduction
The gene for TNFRSF12A was initially recognized as a fibroblast growth factor inducible immediate early response gene Fn14 in mouse NIH 3T3 fibroblasts. Human TNFRSF12A cDNA encodes a 129 amino acid residue type I transmembrane protein with a 27 aa signal peptide, a 53 aa extracellular domain, a 21 aa transmembrane domain and a 28 aa cytoplasmic domain. Human and mouse TNFRSF12A hold 82% aa sequence identity. TNFRSF12 is the tiniest member of the TNF receptor superfamily and has only one cysteine rich region in its extracellular domain. The TNFRSF12A cytoplasmic domain holds one TRAF binding motif which binds TRAFs 1, 2, and 3. TNFRSF12A binds its ligand TWEAK/TNFSF12A with high affinity to initiate a signal transduction cascade which subject to the cell type, causes different cellular responses such as cell death, cell proliferation, and angiogenesis.
Synonyms
Tumor necrosis factor receptor superfamily member 12A, FN14, CD266 antigen, TweakR, tweak-receptor, Fibroblast growth factor-inducible immediate-early response protein 14, FGF-inducible 14, type I transmembrane protein Fn14.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TNFRSF12A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNFRSF12A should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized TNFRSF12A in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
EQAPGTAPCS RGSSWSADLD KCMDCASCRA RPHSDFCLGC AAAPPAPFRL LWP.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interferon Alpha and Beta Receptor Subunit 1 Human Recombinant

IFN-alpha/beta R1, IFNAR1, AVP, IFN-alpha-REC, IFNAR, IFNBR, IFRC, Interferon alpha/beta receptor 1, IFN-R-1, IFN-alpha/beta receptor 1, Cytokine receptor class-II member 1, Cytokine receptor family 2 member 1, CRF2-1, Type I interferon receptor 1.

Product # :

CYT-1138

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SDS-PAGE

Description

IFNAR1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 415 amino acids (28-436a.a.) and having a molecular mass of 47.9kDa. IFNAR1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

IFNAR1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Interferon Alpha And Beta Receptor or IFNAR1, is part of the class II cytokine receptor family. IFNAR1 forms one of the two chains of a receptor for interferons alpha and beta. IFNAR1 binds and activates the receptor that stimulates Janus protein kinases, which then phosphorylate few proteins, including STAT1 & STAT2. Furthermore, IFNAR1 also acts as an antiviral factor.
Synonyms
IFN-alpha/beta R1, IFNAR1, AVP, IFN-alpha-REC, IFNAR, IFNBR, IFRC, Interferon alpha/beta receptor 1, IFN-R-1, IFN-alpha/beta receptor 1, Cytokine receptor class-II member 1, Cytokine receptor family 2 member 1, CRF2-1, Type I interferon receptor 1.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
KNLKSPQKVE VDIIDDNFIL RWNRSDESVG NVTFSFDYQK TGMDNWIKLS GCQNITSTKC NFSSLKLNVY EEIKLRIRAE KENTSSWYEV DSFTPFRKAQ IGPPEVHLEA EDKAIVIHIS PGTKDSVMWA LDGLSFTYSL VIWKNSSGVE ERIENIYSRH KIYKLSPETT YCLKVKAALL TSWKIGVYSP VHCIKTTVEN ELPPPENIEV SVQNQNYVLK WDYTYANMTF QVQWLHAFLK RNPGNHLYKW KQIPDCENVK TTQCVFPQNV FQKGIYLLRV QASDGNNTSF WSEEIKFDTE IQAFLLPPVF NIRSLSDSFH IYIGAPKQSG NTPVIQDYPL IYEIIFWENT SNAERKIIEK KTDVTVPNLK PLTVYCVKAR AHTMDEKLNK SSVFSDAVCE KTKPGNTSKH HHHHH.
Background
What is the molecular weight/Mw of IFNAR1 HUMAN Protein?
IFNAR1 HUMAN Protein has a total Mw of 47.9kDa.

What is the source or expression system of IFNAR1 HUMAN Protein?
Sf9, Insect cells.

What is the Purity of IFNAR1 HUMAN Protein?
IFNAR1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IFNAR1 HUMAN Protein?
The biological functionality of IFNAR1 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IFNAR1 HUMAN Protein?
KNLKSPQKVE VDIIDDNFIL RWNRSDESVG NVTFSFDYQK TGMDNWIKLS GCQNITSTKC NFSSLKLNVY EEIKLRIRAE KENTSSWYEV DSFTPFRKAQ IGPPEVHLEA EDKAIVIHIS PGTKDSVMWA LDGLSFTYSL VIWKNSSGVE ERIENIYSRH KIYKLSPETT YCLKVKAALL TSWKIGVYSP VHCIKTTVEN ELPPPENIEV SVQNQNYVLK WDYTYANMTF QVQWLHAFLK RNPGNHLYKW KQIPDCENVK TTQCVFPQNV FQKGIYLLRV QASDGNNTSF WSEEIKFDTE IQAFLLPPVF NIRSLSDSFH IYIGAPKQSG NTPVIQDYPL IYEIIFWENT SNAERKIIEK KTDVTVPNLK PLTVYCVKAR AHTMDEKLNK SSVFSDAVCE KTKPGNTSKH HHHHH.

What applications can IFNAR1 HUMAN Protein be used in?
IFNAR1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFNAR1 HUMAN Protein?
The endotoxin level is minimal, IFNAR1 HUMAN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Eukaryotic Translation Initiation Factor 3I Human Recombinant, Sf9

eIF3-beta, eIF3-p36, EIF3S2, PRO2242, TRIP-1, TRIP1, Eukaryotic translation initiationfactor 3 subunit I, eIF3i, TGF-beta receptor-interacting protein 1, eIF-3-beta.

Product # :

PRO-2611

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Description

EIF3I Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 331 amino acids (1-325 a.a) and having a molecular mass of 37.3kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).EIF3I is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

EIF3I protein solution (0.25mg/ml) 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 40% Glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Eukaryotic translation initiation factor 3, subunit I (EIF3I) is part of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is essential for numerous steps in the initiation of protein synthesis. The eIF-3 complex links with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2: GTP: methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also essential for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. Among the diseases associated with EIF3I are clonorchiasis, and tonsillitis.
Synonyms
eIF3-beta, eIF3-p36, EIF3S2, PRO2242, TRIP-1, TRIP1, Eukaryotic translation initiation
factor 3 subunit I, eIF3i, TGF-beta receptor-interacting protein 1, eIF-3-beta.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MKPILLQGHE RSITQIKYNR EGDLLFTVAK DPIVNVWYSV NGERLGTYMG HTGAVWCVDA
DWDTKHVLTG SADNSCRLWD CETGKQLALL KTNSAVRTCG FDFGGNIIMF STDKQMGYQC
FVSFFDLRDP SQIDNNEPYM KIPCNDSKIT SAVWGPLGEC IIAGHESGEL NQYSAKSGEV
LVNVKEHSRQ INDIQLSRDM TMFVTASKDN TAKLFDSTTL EHQKTFRTER PVNSAALSPN
YDHVVLGGGQ EAMDVTTTST RIGKFEARFF HLAFEEEFGR VKGHFGPINS VAFHPDGKSY SSGGEDGYVR IHYFDPQYFE FEFEAHHHHH H.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Retinol Binding Protein-5 Human Recombinant

Retinol-binding protein 5, Cellular retinol-binding protein III, CRBP-III, HRBPiso, RBP5, CRBP3, CRBPIII.

Product # :

CYT-650

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Description

RBP5 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 155 amino acids (1-135 a.a.) and having a molecular mass of 18.1kDa. The RBP5 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The RBP5 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT and 100mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
RBP5 is a member of the Retinol-binding proteins family. Estimation of retinol-binding protein is used to determine visceral protein mass in nutritional studies related to health. RBP5 has a higher expression in the adult kidney and liver and to a lesser extent in the adult and fetal spleen, adult lymph nodes and appendix, and fetal liver and kidney. RBP5 expression is strongly decreased in hepatocellular carcinoma tissues.
Synonyms
Retinol-binding protein 5, Cellular retinol-binding protein III, CRBP-III, HRBPiso, RBP5, CRBP3, CRBPIII.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPPNLTGYYR FVSQKNMEDY LQALNISLAV RKIALLLKPD KEIEHQGNHM TVRTLSTFRN YTVQFDVGVE FEEDLRSVDG RKCQTIVTWE EEHLVCVQKG EVPNRGWRHW LEGEMLYLEL TARDAVCEQV FRKVR.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Prothrombin Bovine

Coagulation factor II, Prothrombin, F2.

Product # :

PRO-2759

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Description

Prothrombin bovine native.

Source

Bovine Plasma.

Formulation

The bovine prothrombin was lyophilized with no additives.

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Introduction
Prothrombin produced in the liver is a vitamin K-dependent plasma protein. Before prothrombin is secreted into the plasma it goes through post translational modification by vitamin K-dependent carboxylase. The vitamin K-dependent carboxylase convertsprothrombin to 10 glutamic acid residues to gamma carboxyglutamic acid. Prothrombin comprises of 2 kringle regions which are found among residues a.a. 40 & 270 of the mature plasma protein and substitute the growth factor domains located in numerous plasma serine proteases.
Synonyms
Coagulation factor II, Prothrombin, F2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Bovine Prothrombin although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Prothrombin should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles
Solubility
It is recommended to reconstitute the lyophilized Bovine Prothrombin in sterile 0.9% NaCl

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

BAFF (BLyS) Receptor Human Recombinant, HEK

TNFRSF13C, CD268, BAFF-R, MGC138235, B cell-activating factor receptor.

Product # :

CYT-1224

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Description

BAFFR Human Recombinant is a single, glycosylated, polypeptide chain (1-78 a.a) containing a total of 314 amino acids and having a molecular mass of 34.4 kDa. BAFFR is fused to 233 a.a hIgG-Tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The BAFFR solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 is ≤0.7 ug/ml, measured by its ability in a functional ELISA with BAFF Human.

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Synonyms
TNFRSF13C, CD268, BAFF-R, MGC138235, B cell-activating factor receptor.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
DGSMRRGPRS LRGRDAPAPT PCVPAECFDL LVRHCVACGL LRTPRPKPAG ASSPAPRTAL QPQESVGAGA GEAALPLPGL LLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGK.
Background
B-cell Activating Factor (BAFF) and its corresponding receptor, BAFF-R, are integral components of the immune system, orchestrating crucial processes in B-cell survival, maturation, and differentiation. As we delve into the intricate world of immunology, the study of BAFF and its receptor has unveiled essential pathways that govern the immune responses in health and disease. This research investigates the multifaceted role of BAFF Receptor Protein, shedding light on its structural complexities, signaling mechanisms, and its pivotal contributions to immune regulation. By exploring the interactions between BAFF and its receptor, scientists aim to decipher the delicate balance that underlies immune homeostasis and explore potential therapeutic avenues.
Structural Architecture of BAFF Receptor Protein:
BAFF Receptor, a transmembrane protein predominantly expressed on B cells, belongs to the tumor necrosis factor receptor (TNFR) superfamily. Its intricate structure involves various domains, each playing a unique role in ligand binding, receptor activation, and downstream signaling. Understanding the structural intricacies of BAFF Receptor is paramount to unraveling the molecular events that govern B-cell fate decisions and immune responses.
Physiological Significance in B-Cell Biology:
BAFF Receptor, upon binding with its ligand BAFF, initiates a cascade of events critical for B-cell survival and function. This interaction promotes B-cell maturation, prevents premature apoptosis, and influences the formation of immune synapses. Additionally, BAFF Receptor signaling is tightly regulated to prevent excessive B-cell activation, ensuring immune tolerance and preventing autoimmune responses. Disruptions in these pathways can lead to autoimmune disorders, underscoring the crucial role of BAFF Receptor in maintaining immune equilibrium.
Regulation of Immune Responses:
BAFF Receptor signaling not only affects B-cell development but also has broader implications for immune responses. By modulating antibody production, B-cell activation, and immune memory, BAFF Receptor plays a vital role in shaping adaptive immunity. Its dysregulation has been implicated in various autoimmune conditions, making it an attractive target for therapeutic interventions aimed at restoring immune balance.
BAFF Receptor as a Therapeutic Target:
The intricate involvement of BAFF Receptor in autoimmune diseases, such as rheumatoid arthritis and systemic lupus erythematosus, has positioned it as a promising therapeutic target. Researchers are exploring monoclonal antibodies and other targeted therapies that aim to modulate BAFF Receptor signaling, providing a new frontier in autoimmune disease management. Additionally, understanding the BAFF-BAFF Receptor axis offers potential insights into the development of vaccines and immunotherapies, fostering innovative approaches in the fight against infectious diseases and malignancies.
BAFF Receptor Protein, as a key player in immune regulation, embodies the complexities of immunology. Its interactions with BAFF orchestrate fundamental processes in B-cell biology and adaptive immunity. As scientists unravel the intricate signaling pathways and structural nuances of BAFF Receptor, they pave the way for novel therapeutic strategies and innovative treatments for autoimmune disorders and beyond. This research not only deepens our understanding of immune regulation but also holds the promise of transformative advancements in immunotherapy, ultimately shaping the future of immune-related healthcare.
What is the molecular weight/Mw of BAFF-R Protein?
BAFF-R Protein has a total Mw of 34.4kDa.

What is the source or expression system of BAFF-R Protein?
HEK293 Cells.

What is the Purity of BAFF-R Protein?
BAFF-R Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BAFF-R Protein?
The ED50 is ≤0.7 ug/ml, measured by its ability in a functional ELISA with BAFF Human.

What is the amino acid sequence of BAFF-R Protein?
DGSMRRGPRS LRGRDAPAPT PCVPAECFDL LVRHCVACGL LRTPRPKPAG ASSPAPRTAL QPQESVGAGA GEAALPLPGL LLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGK.

What applications can BAFF-R Protein be used in?
BAFF-R Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BAFF-R Protein?
The endotoxin level is minimal, BAFF-R Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

OX40 Ligand Human Recombinant

Tumor necrosis factor ligand superfamily member 4, OX40 ligand, OX40L, OX-40L, CD252, Tnfsf4, Ox40l, Txgp1l, gp3, OX4, Ath-1, Ath1, CD134L, gp34, Tnlg2b, Txgp1l.

Product # :

CYT-1226

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description
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Description

OX40L Human Recombinant is a single, glycosylated, polypeptide chain (51-183 a.a) containing a total of139 amino acids and having a molecular mass of 16.2 kDa. OX40L is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The OX40L solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured by its binding ability in a functional ELISA with Human OX40/TNFRSF4.

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Synonyms
Tumor necrosis factor ligand superfamily member 4, OX40 ligand, OX40L, OX-40L, CD252, Tnfsf4, Ox40l, Txgp1l, gp3, OX4, Ath-1, Ath1, CD134L, gp34, Tnlg2b, Txgp1l.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
QVSHRYPRIQ SIKVQFTEYK KEKGFILTSQ KEDEIMKVQN NSVIINCDGF YLISLKGYFS QEVNISLHYQ KDEEPLFQLK KVRSVNSLMV ASLTYKDKVY LNVTTDNTSL DDFHVNGGEL ILIHQNPGEF CVLHHHHHH.
Background
OX40 Ligand (OX40L), a member of the tumor necrosis factor (TNF) superfamily, plays a pivotal role in regulating immune responses and orchestrating the delicate balance between activation and tolerance. The human recombinant form of OX40L has emerged as a potent tool in immunology, offering insights into its molecular intricacies and potential applications in therapeutic interventions. This research embarks on a journey to unravel the multifaceted role of OX40L Human Recombinant, shedding light on its structural attributes, signaling pathways, and its promising avenues in immunotherapy. By delving into the properties of OX40L, scientists aim to expand our understanding of immune modulation and open new frontiers in the treatment of immune-related disorders.
Structural Insights into OX40L Human Recombinant:
OX40L, as a trimeric transmembrane protein, exhibits a unique structural configuration that governs its interactions with the OX40 receptor on T cells. The human recombinant form, engineered for controlled study, provides a window into the three-dimensional intricacies of the ligand. Understanding its structure is pivotal for deciphering how OX40L engages with its receptor and modulates immune responses.
Immunomodulatory Signaling Pathways:
OX40L binding to its cognate receptor OX40 on T cells triggers intricate signaling cascades that impact immune cell activation, proliferation, and cytokine production. The OX40-OX40L axis is a crucial regulator of T cell function, influencing both effector and regulatory T cell responses. Unraveling the specific pathways activated by OX40L Human Recombinant provides valuable insights into the modulation of immune responses in health and disease.
Applications in Immunotherapy:
The immunomodulatory properties of OX40L make it an attractive candidate for therapeutic interventions. OX40L Human Recombinant, in preclinical and clinical studies, is being explored for its potential in enhancing antitumor immune responses. By harnessing the ligand's ability to stimulate effector T cells and memory T cell formation, researchers aim to develop novel immunotherapies for cancer and other immune-related disorders.
OX40L in Autoimmune Diseases:
Conversely, OX40L's role in autoimmune diseases has spurred investigations into its inhibition as a therapeutic strategy. Blocking the OX40-OX40L interaction has shown promise in mitigating autoimmune responses, presenting a potential avenue for the development of treatments for conditions such as rheumatoid arthritis and inflammatory bowel disease.
While the potential of OX40L Human Recombinant in immunotherapy is promising, challenges persist. Fine-tuning its applications, understanding potential side effects, and optimizing dosages are critical considerations for translational success. Additionally, comprehending the context-dependent nature of OX40L signaling is essential for tailoring therapeutic strategies to specific diseases and patient profiles.
OX40L Human Recombinant stands at the forefront of immunomodulation research, offering a lens through which we can unravel the complexities of immune responses. Its structural insights, signaling pathways, and therapeutic applications position it as a key player in the evolving landscape of immunotherapy. As researchers continue to dissect the molecular nuances of OX40L, they not only expand our understanding of immune regulation but also pave the way for transformative advancements in the treatment of cancer and autoimmune diseases, shaping the future of precision medicine and immunotherapy.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Leptin Chicken Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-505

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Leptin Chicken Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 145 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

Purity

Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its activity is however 5-10 fold lower as compared to mammalian leptins.

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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Cys-Gln.
Recombinant Chicken leptin was produced according to the a.a. sequence published by the groups of Taouis & McMutry, see Raver et al. Protein Expr Purif. 1998 Dec; 14(3):403-8.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.19 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC,using calibrated solution of Leptin Chicken as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Glia Maturation Factor Beta Human His Tag Recombinant

GMF, GMF beta.

Product # :

CYT-726

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

GMFB Human Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 162 amino acids (1-142 a.a.)and having a total molecular mass of 18.8 kDa. GMGB is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GMFB 1mg/ml protein solution contains 20mM Tris-HCL pH-8, 1mM DTT, 0.1M NaCl and 10% Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GMFB is part of the GMF subfamily of the larger actin-binding protein ADF family. GMFB is phosphorylated after phorbol ester stimulation, and is crucial for the nervous system. GMFB causes brain cell differentiation, stimulates neural regeneration and inhibits tumor cell proliferation. GMFB overexpression in astrocytes results in the increase of BDNF production. GMFB expression is increased by exercise, thus BDNF is important for exercise-induction of BDNF.
Synonyms
GMF, GMF beta.
Physical Appearance
Sterile Filtered colorless clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSESLVVCDV AEDLVEKLRK FRFRKETNNA AIIMKIDKDK RLVVLDEELE GISPDELKDE LPERQPRFIV
YSYKYQHDDG RVSYPLCFIF SSPVGCKPEQ QMMYAGSKNK LVQTAELTKV FEIRNTEDLT EEWLREKLGF FH.
Background
What is the molecular weight/Mw of GMFB HIS HUMAN Protein?
GMFB HIS HUMAN Protein has a total Mw of 18.8kDa.

What is the source or expression system of GMFB HIS HUMAN Protein?
Escherichia Coli.

What is the Purity of GMFB HIS HUMAN Protein?
GMFB HIS HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GMFB HIS HUMAN Protein?
The biological functionality of GMFB HIS HUMAN Protein will be determined in the future.

What is the amino acid sequence of GMFB HIS HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MSESLVVCDV AEDLVEKLRK FRFRKETNNA AIIMKIDKDK RLVVLDEELE GISPDELKDE LPERQPRFIV
YSYKYQHDDG RVSYPLCFIF SSPVGCKPEQ QMMYAGSKNK LVQTAELTKV FEIRNTEDLT EEWLREKLGF FH.

What applications can GMFB HIS HUMAN Protein be used in?
GMFB HIS HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GMFB HIS HUMAN Protein?
The endotoxin level is minimal, GMFB HIS HUMAN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Tumor Necrosis Factor-Alpha Rabbit Recombinant

Tumor necrosis factor, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, TNFA, TNFSF2.

Product # :

CYT-008

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Tumor Necrosis Factor-a Rabbit Recombinant consists of three identical polypeptide chains of 158 amino acids combined to form a compact, bell-shaped homotrimer. TNF-alpha was produced in E.Coli is a non-glycosylated, polypeptide chain having a molecular mass of 17.4 kDa for the individual subunit. The TNF-alpha is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

TNF-alpha Rabbit was lyophilized after extensive dialysis against 20mM PB, pH7.4, 300mM NaCl.

Purity

Greater than 95% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is less than 0.03ng/ml, corresponding to a Specific Activity of 30,000,000 IU/mg.

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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.
Synonyms
Tumor necrosis factor, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, TNFA, TNFSF2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Tumor Necrosis Factor-alpha in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ser-Ala-Ser-Arg.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interleukin-9 Mouse Recombinant

P40, HP40, T-cell growth factor p40, IL-9, P40 cytokine.

Product # :

CYT-373

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interleukin-9 Mouse Recombinant produced in E.Coli is a single, non-glycosylated single polypeptide chain containing 127 amino acids and having a molecular mass of 14.3kDa. The IL-9 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution 10mM Na2PO4, pH 7.5.

Purity

Greater than 96.0% as determined by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of human MO7e cells is < 0.5 ng/ml, corresponding to a Specific Activity of 2,000,000IU/mg.

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Introduction
Factor that is thought to be a regulator of hematopoiesis. It has been shown to enhance the growth of human mast cells and megakaryoblastic leukemic cells as well as murine helper t-cell clones. IL-9 is a glycoprotein with a molecular weight of 32-39 that is derived from T-cells, and maps to human chromosome 5.
Synonyms
P40, HP40, T-cell growth factor p40, IL-9, P40 cytokine.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-9 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL9 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin 9 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQRCSTTWGI RDTNYLIENL KDDPPSKCSC SGNVTSCLCL SVPTDDCTTP CYREGLLQLT NATQKSRLLP VFHRVKRIVE VLKNITCPSF SCEKPCNQTM AGNTMSFLKS LLGTFQKTEM QRQKSRP.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.6 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-9 as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Growth differentiation factor 5 Human Recombinant, His Tag

Cartilage-derived morphogenetic protein-1, CDMP-1, LAP4, SYNS2, GDF-5, Radotermin, CDMP1, GDF5, Growth differentiation factor 5, BMP-14.

Product # :

CYT-653

Price :

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Shipping Method :

Shipped with Ice Packs

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Description

GDF5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids (382-501 a.a.) and having a total molecular mass of 15.8 kDa. GDF5 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GDF5 solution contains 10mM sodium citrate pH-3.5 and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GDF-5 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. Mutations in this gene are associated with acromesomelic dysplasia, Hunter-Thompson type; brachydactyly, type C; and chondrodysplasia, Grebe type. These associations confirm that the gene product plays a role in skeletal development.
Synonyms
Cartilage-derived morphogenetic protein-1, CDMP-1, LAP4, SYNS2, GDF-5, Radotermin, CDMP1, GDF5, Growth differentiation factor 5, BMP-14.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAPLATRQGK RPSKNLKARC SRKALHVNFK DMGWDDWIIA PLEYEAFHCE GLCEFPLRSH LEPTNHAVIQ TLMNSMDPES TPPTCCVPTR LSPISILFID SANNVVYKQY EDMVVESCGC R.
Background
What is the molecular weight/Mw of GDF5 HUMAN, HIS Protein?
GDF5 HUMAN, HIS Protein has a total Mw of 15.8kDa.

What is the source or expression system of GDF5 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of GDF5 HUMAN, HIS Protein?
GDF5 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF5 HUMAN, HIS Protein?
The biological functionality of GDF5 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of GDF5 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MAPLATRQGK RPSKNLKARC SRKALHVNFK DMGWDDWIIA PLEYEAFHCE GLCEFPLRSH LEPTNHAVIQ TLMNSMDPES TPPTCCVPTR LSPISILFID SANNVVYKQY EDMVVESCGC R.

What applications can GDF5 HUMAN, HIS Protein be used in?
GDF5 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF5 HUMAN, HIS Protein?
The endotoxin level is minimal, GDF5 HUMAN, HIS Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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