Search: 1000 results found for "Macrophage Migration Inhibitory Factor"

Description:

Galectin-3 Mouse Recombinant, BioActive

Lectin galactose binding soluble 3, Lectin, galactose binding, soluble 3, CBP35, GAL3, GALBP, GALIG, LGALS2, MAC2.

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CYT-1151

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Description

LGALS3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 287 amino acids ( 1-264 a.a) and having a molecular mass of 29.8kDa.LGALS3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

LGALS3 protein (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol,1mM DTT and 2mM EDTA.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to agglutinate human red blood cells. The ED50 for this effect is ≥ 25ug/ml.

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Introduction
Galectin 3, or LGALS3, is a protein which belongs to the animal lectins family, that binds betagalactoside residues selectively. LGALS3 is originated and leaves cells through ectocytosis. The protein is capable of inhibition apoptosis and the development of cancer. Galectin 3 is found in epithelial tissues in organisms, it can be located in dendritic cells, Kupffer cells, macrophages etc. LGALS3 levels elevated when inflammation is generating, cell proliferation, trans-activation by viral proteins and cell differentiation.
Synonyms
Lectin galactose binding soluble 3, Lectin, galactose binding, soluble 3, CBP35, GAL3, GALBP, GALIG, LGALS2, MAC2.
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 MGSMADSFSL NDALAGSGNP NPQGYPGAWG NQPGAGGYPG AAYPGAYPGQ APPGAYPGQA PPGAYPGQAP PSAYPGPTAP GAYPGPTAPG AYPGSTAPGA FPGQPGAPGA YPSAPGGYPA AGPYGVPAGP LTVPYDLPLP GGVMPRMLIT IMGTVKPNAN RIVLDFRRGN DVAFHFNPRF NENNRRVIVC NTKQDNNWGK EERQSAFPFE SGKPFKIQVL VEADHFKVAV NDAHLLQYNH RMKNLREISQ LGISGDITLT SANHAMI.
Background
What is the molecular weight/Mw of LGALS3 MOUSE Protein?
LGALS3 MOUSE Protein has a total Mw of 29.8kDa.

What is the source or expression system of LGALS3 MOUSE Protein?
Escherichia Coli.

What is the Purity of LGALS3 MOUSE Protein?
LGALS3 MOUSE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of LGALS3 MOUSE Protein?
Measured by its ability to agglutinate human red blood cells. The ED50 for this effect is ≥ 25ug/ml.

What is the amino acid sequence of LGALS3 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMADSFSL NDALAGSGNP NPQGYPGAWG NQPGAGGYPG AAYPGAYPGQ APPGAYPGQA PPGAYPGQAP PSAYPGPTAP GAYPGPTAPG AYPGSTAPGA FPGQPGAPGA YPSAPGGYPA AGPYGVPAGP LTVPYDLPLP GGVMPRMLIT IMGTVKPNAN RIVLDFRRGN DVAFHFNPRF NENNRRVIVC NTKQDNNWGK EERQSAFPFE SGKPFKIQVL VEADHFKVAV NDAHLLQYNH RMKNLREISQ LGISGDITLT SANHAMI.

What applications can LGALS3 MOUSE Protein be used in?
LGALS3 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

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:

TRAF Family Member-Associated NFKB Activator Human Recombinant

TRAF, TRAF2, TRAF-interacting protein, ITRAF.

Product # :

PRO-1348

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Description

TANK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 448 amino acids (1-425a.a) and having a molecular mass of 50.2kDa. TANK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TANK protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
TRAF Family Member-Associated NFKB Activator (TANK) is located in the cytoplasm and binds Either TRAF1, TRAF2 or TRAF3. TANK is an inhibitor of TRAF function which regulates TRAF protein activity via sequestering TRAFs in a dormant position in the cytoplasm. Overexpression of TANK, inhibits TRAF2-mediated NF-Kappa-B activation signaled by CD40 and both TNF receptors and also inhibits LMP1-mediated NFkappa-B activation by blocking the connection of TRAF2 with LMP1.
Synonyms
TRAF, TRAF2, TRAF-interacting protein, ITRAF.
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 MGSMDKNIGE QLNKAYEAFR QACMDRDSAV KELQQKTENY EQRIREQQEQ LSLQQTIIDK LKSQLLLVNS TQDNNYGCVP LLEDSETRKN NLTLDQPQDK VISGIAREKL PKVRRQEVSS PRKETSARSL GSPLLHERGN IEKTFWDLKE EFHKICMLAK AQKDHLSKLN IPDTATETQC SVPIQCTDKT DKQEALFKPQ AKDDINRGAP SITSVTPRGL CRDEEDTSFE SLSKFNVKFP PMDNDSTFLH STPERPGILS PATSEAVCQE KFNMEFRDNP GNFVKTEETL FEIQGIDPIA SAIQNLKTTD KTKPSNLVNT CIRTTLDRAA CLPPGDHNAL YVNSFPLLDP SDAPFPSLDS PGKAIRGPQQ PIWKPFPNQD SDSVVLSGTD SELHIPRVCE FCQAVFPPSI TSRGDFLRHL NSHFNGET.

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 Triple Antagonist (D23L) Pegylated Mouse Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-1242

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Description

Leptin Antagonist Triple Mutant D23L Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus. The Leptin antagonist was mutated, resulting in L39A/D40A/F41A mutant. The Mouse Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Mouse Leptin triple anatagonist runs as a 48 kDa. Leptin Antagonist Triple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

The Mouse Leptin triple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

Purity

Greater than 99.0% as determined by:

(a) Gel filtration analysis.

(b) Analysis by SDS-PAGE.

Biological Activity

Leptin Antagonist Triple Mutant D23L Mouse Recombinant is capable of stimulating proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is only slightly lower than the non-pegylated recombinant mouse leptin but in vivo it has profound weight reducing effect (as compared to the non-pegylated recombinant mouse leptin), resulting mainly from reduced food intake.

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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
Background
Leptin is a hormone which mainly produced by adipocytes . Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin effects mainly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor is found on a wide range of cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.

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:

Matrix Metalloproteinase-28 Human Recombinant

EPILYSIN, MM28, MMP-28, MMP25, Matrix metalloproteinase-28, MMP28.

Product # :

ENZ-768

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Description

MMP28 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 421 amino acids (123-520a.a) and having a molecular mass of 47.3kDa. MMP28 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MMP28 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
MMP28, which belongs to the matrix metalloproteinase (MMP) family, takes part in the breakdown of extracellular matrix for both normal physiological processes, such as embryonic development, reproduction and tissue remodeling, and disease processes, like asthma and metastasis. MMP28 is a secreted enzyme which degrades casein. MMP28 participates in tissue homeostasis and in wound repair.
Synonyms
EPILYSIN, MM28, MMP-28, MMP25, Matrix metalloproteinase-28, MMP28.
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 MGSFAKQGNK WYKQHLSYRL VNWPEHLPEP AVRGAVRAAF QLWSNVSALE FWEAPATGPA DIRLTFFQGD HNDGLGNAFD GPGGALAHAF LPRRGEAHFD QDERWSLSRR RGRNLFVVLA HEIGHTLGLT HSPAPRALMA PYYKRLGRDA LLSWDDVLAV QSLYGKPLGG SVAVQLPGKL FTDFETWDSY SPQGRRPETQ GPKYCHSSFD AITVDRQQQL YIFKGSHFWE VAADGNVSEP RPLQERWVGL PPNIEAAAVS LNDGDFYFFK GGRCWRFRGP KPVWGLPQLC RAGGLPRHPD AALFFPPLRR LILFKGARYY VLARGGLQVE PYYPRSLQDW GGIPEEVSGA LPRPDGSIIF FRDDRYWRLD QAKLQATTSG RWATELPWMG CWHANSGSAL F.

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:

N-Methylpurine-DNA Glycosylase Human Recombinant

DNA-3-methyladenine glycosylase, 3-alkyladenine DNA glycosylase, 3-methyladenine DNA glycosidase, ADPG, N-methylpurine-DNA glycosylase, MPG, AAG, ANPG, MID1, MDG, PIG11, PIG16, CRA36.1.

Product # :

ENZ-151

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Description

MPG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 306 amino acids (1-298 a.a.) and having a molecular mass of 33.9kDa (Molecular weight on SDS-PAGE will appear higher).MPG is fused to an 8 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MPG protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol, 200mM NaCl and 1mM EDTA.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
DNA-3-methyladenine glycosylase (MPG) is a member of the DNA glycosylase MPG family. MPG initiates base excision repair in DNA by removing a wide variety of alkylated, deaminated, and lipid peroxidation-induced purine adducts.
Synonyms
DNA-3-methyladenine glycosylase, 3-alkyladenine DNA glycosylase, 3-methyladenine DNA glycosidase, ADPG, N-methylpurine-DNA glycosylase, MPG, AAG, ANPG, MID1, MDG, PIG11, PIG16, CRA36.1.
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
MVTPALQMKK PKQFCRRMGQ KKQRPARAGQ PHSSSDAAQA PAEQPHSSSD AAQAPCPRER CLGPPTTPGP YRSIYFSSPK GHLTRLGLEF FDQPAVPLAR AFLGQVLVRR LPNGTELRGR IVETEAYLGP EDEAAHSRGG RQTPRNRGMF MKPGTLYVYI IYGMYFCMNI SSQGDGACVL LRALEPLEGL ETMRQLRSTL RKGTASRVLK DRELCSGPSK LCQALAINKS FDQRDLAQDE AVWLERGPLE PSEPAVVAAA RVGVGHAGEW ARKPLRFYVR GSPWVSVVDR VAEQDTQALE HHHHHH.

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:

TEK Tyrosine Kinase Endothelial Fc Chimera Human Recombinant

Angiopoietin-1 receptor precursor, Tyrosine-protein kinase receptor TIE-2, hTIE2, Tyrosine-protein kinase receptor TEK, p140 TEK, Tunica interna endothelial cell kinase, CD202b, VMCM, VMCM1, TIE2.

Product # :

PKA-248

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Description

Soluble TEK Human Recombinant fused with the Fc part of human IgG1 produced in baculovirus is a monomeric, glycosylated, polypeptide containing 730 amino acids and having a total molecular mass of 250 kDa. Human TIE-2/Fc monomer has a calculated molecular mass of approximately 125 kDa. As a result of glycosylation, the recombinant protein migrates as an approximately 140 kDa protein in SDS-PAGE under reducing conditions.The TEK Fc Chimera is purified by proprietary chromatographic techniques.

Source

Insect Cells.

Formulation

TEK Fc Chimera was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.

Purity

Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
TIE-1 (tyrosine kinase with Ig and EGF homology domains 1) and TIE-2/Tek comprise a receptor tyrosine kinase (RTK) subfamily with unique structural characteristics: two immunoglobulin-like domains flanking three epidermal growth factor (EGF)-like domains and followed by three fibronectin type III-like repeats in the extracellular region and a split tyrosine kinase domain in the cytoplasmic region. These receptors are expressed primarily on endothelial and hematopoietic progenitor cells and play critical roles in angiogenesis, vasculogenesis and hematopoiesis. Human TIE-1 cDNA encodes a 1122 amino acid (aa) residue precursor protein with an 18 residue putative signal peptide, a 726 residue extracellular domain and a 353 residue cytoplasmic domain. Two ligands, angiopoietin-1 (Ang1) and angiopoietin-2 (Ang2), which bind TIE-2 with high-affinity have been identified. Ang2 has been reported to act as an antagonist for Ang1. Mice engineered to overexpress Ang2 or to lack Ang1 or Tie-1 display similar angiogenic defects.
Synonyms
Angiopoietin-1 receptor precursor, Tyrosine-protein kinase receptor TIE-2, hTIE2, Tyrosine-protein kinase receptor TEK, p140 TEK, Tunica interna endothelial cell kinase, CD202b, VMCM, VMCM1, TIE2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized sTIE-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TEK 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 TIE-2 Fc Chimera in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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:

Flt3 Ligand Porcine Recombinant

Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.

Product # :

CYT-1041

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Description

Flt3-Ligand Porcine Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of approximately 17.3kDa. Flt3-Ligand is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein is lyophilized with 10mM Sodium Phosphate pH-7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.
Synonyms
Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Porcine Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3-Ligand 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 Flt3-L in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSPDCSFPHS PISSTFANTI RQLSDYLLQD YPVTVASNLQ DDELCGAFWR LVLAQRWMGQ LKTVAGSQMQ KLLEAVNTEI VFVTSCALQP LPSCLRFVQA NISHLLQDTS QQLVALKPWI TRRNFSRCLE LQCQPDPSTL LPPRSPGALE ATSLP.
Background
What is the molecular weight/Mw of FLT3 LIGAND PORCINE Protein?
FLT3 LIGAND PORCINE Protein has a total Mw of 17.3kDa.

What is the source or expression system of FLT3 LIGAND PORCINE Protein?
Escherichia Coli.

What is the Purity of FLT3 LIGAND PORCINE Protein?
FLT3 LIGAND PORCINE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FLT3 LIGAND PORCINE Protein?
The biological functionality of FLT3 LIGAND PORCINE Protein will be determined in the future.

What is the amino acid sequence of FLT3 LIGAND PORCINE Protein?
MSPDCSFPHS PISSTFANTI RQLSDYLLQD YPVTVASNLQ DDELCGAFWR LVLAQRWMGQ LKTVAGSQMQ KLLEAVNTEI VFVTSCALQP LPSCLRFVQA NISHLLQDTS QQLVALKPWI TRRNFSRCLE LQCQPDPSTL LPPRSPGALE ATSLP.

What applications can FLT3 LIGAND PORCINE Protein be used in?
FLT3 LIGAND PORCINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FLT3 LIGAND PORCINE Protein?
The endotoxin level is minimal, FLT3 LIGAND PORCINE 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:

Mitogen-Activated Protein Kinase 9 Human Recombinant

Mitogen-activated protein kinase 9, MAP kinase 9, MAPK 9, JNK-55, Stress-activated protein kinase 1a, SAPK1a, Stress-activated protein kinase JNK2, c-Jun N-terminal kinase 2, MAPK9, JNK2, PRKM9, SAPK, p54a, JNK2A, JNK2B, JNK2BETA, p54aSAPK, JNK2ALPHA.

Product # :

PKA-039

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Description

MAPK9 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 406 amino acids (1-382 a.a) and having a molecular mass of 46.6kDa.MAPK9 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MAPK9 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Mitogen-activated protein kinase 9 (MAPK9) belongs to the MAP kinase family. MAP kinases function as an integration point for numerous biochemical signals, and are involved in a broad variety of cellular processes such as proliferation, differentiation, transcription regulation and development. MAPK9 targets specific transcription factors, and consequently mediates immediate-early gene expression in response to diverse cell stimuli. As an active dimer, MAPK9 can translocate to the nucleus and control transcription through its effects on c-Jun, ATF-2, and other transcription factors. MAPK9 blocks the ubiquitination of tumor suppressor p53, and so it increases the stability of p53 in nonstressed cells.
Synonyms
Mitogen-activated protein kinase 9, MAP kinase 9, MAPK 9, JNK-55, Stress-activated protein kinase 1a, SAPK1a, Stress-activated protein kinase JNK2, c-Jun N-terminal kinase 2, MAPK9, JNK2, PRKM9, SAPK, p54a, JNK2A, JNK2B, JNK2BETA, p54aSAPK, JNK2ALPHA.
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 MGSHMSDSKC DSQFYSVQVA DSTFTVLKRY QQLKPIGSGA QGIVCAAFDT VLGINVAVKK LSRPFQNQTH AKRAYRELVL LKCVNHKNII SLLNVFTPQK TLEEFQDVYL VMELMDANLC QVIHMELDHE RMSYLLYQML CGIKHLHSAG IIHRDLKPSN IVVKSDCTLK ILDFGLARTA CTNFMMTPYV VTRYYRAPEV ILGMGYKENV DIWSVGCIMG ELVKGCVIFQ GTDHIDQWNK VIEQLGTPSA EFMKKLQPTV RNYVENRPKY PGIKFEELFP DWIFPSESER DKIKTSQARD LLSKMLVIDP DKRISVDEAL RHPYITVWYD PAEAEAPPPQ IYDAQLEERE HAIEEWKELI YKEVMDWEER SKNGVVKDQP SAQMQQ.

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:

Zinc Finger HIT-Type Containing 3 Human Recombinant

Zinc finger HIT domain-containing protein 3, HNF-4a coactivator, Thyroid hormone receptor interactor 3, Thyroid receptor-interacting protein 3, TR-interacting protein 3, TRIP-3, ZNHIT3, TRIP3, Zinc finger, HIT-type containing 3.

Product # :

PRO-1699

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Description

ZNHIT3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 178 amino acids (1-155) and having a molecular mass of 20 kDa.ZNHIT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The ZNHIT3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Zinc Finger HIT-Type Containing 3 (ZNHIT3) which contains one HIT-type zinc finger, requires the presence of thyroid hormone for its interaction. Thyroid receptor interacting proteins particularly interact with the ligand binding domain of the thyroid receptor (TR).
Synonyms
Zinc finger HIT domain-containing protein 3, HNF-4a coactivator, Thyroid hormone receptor interactor 3, Thyroid receptor-interacting protein 3, TR-interacting protein 3, TRIP-3, ZNHIT3, TRIP3, Zinc finger, HIT-type containing 3.
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 MGSMASLKCS TVVCVICLEK PKYRCPACRV PYCSVVCFRK HKEQCNPETR PVEKKIRSAL PTKTVKPVEN KDDDDSIADF LNSDEEEDRV SLQNLKNLGE SATLRSLLLN PHLRQLMVNL DQGEDKAKLM RAYMQEPLFV EFADCCLGIV EPSQNEES.

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:

Bone Morphogenetic protein-8b Human Recombinant

Bone morphogenetic protein 8B, BMP-8, BMP-8B, Osteogenic protein 2, OP-2, BMP8B, BMP8, Bone Morphogenetic protein-8b, OP2.

Product # :

CYT-830

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sds-page

Description

BMP8B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 162 amino acids (264-402a.a.) and having a molecular mass of 18.1kDa.BMP8B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

BMP8B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

sds-page

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Introduction
Bone Morphogenetic protein-8b (BMP8B) belongs to a family of secreted signaling molecules which can induce ectopic bone growth. BMP8B is known for having a possible bone inductive activity as it is related to BMP5 and BMP7. BMP8B is the osteoinductive factor accountable for epithelial osteogenesis.
Synonyms
Bone morphogenetic protein 8B, BMP-8, BMP-8B, Osteogenic protein 2, OP-2, BMP8B, BMP8, Bone Morphogenetic protein-8b, OP2.
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 MGSAVRPLRR RQPKKSNELP QANRLPGIFD DVHGSHGRQV CRRHELYVSF QDLGWLDWVI APQGYSAYYC EGECSFPLDS CMNATNHAIL QSLVHLMMPD AVPKACCAPT KLSATSVLYY DSSNNVILRK HRNMVVKACG CH.
Background
Bone Morphogenetic Protein-8B Human Recombinant: Unveiling the Potential for Regenerative Medicine and Tissue Engineering
Abstract:
Bone Morphogenetic Protein-8B (BMP-8B) human recombinant is a key member of the bone morphogenetic protein family, renowned for its crucial role in tissue development, regeneration, and repair. This research paper aims to provide a comprehensive analysis of BMP-8B, including its characteristics, signaling pathways, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of BMP-8B human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine and tissue engineering.
Introduction:
Regenerative medicine and tissue engineering offer promising solutions to address the challenges of tissue repair and regeneration. BMP-8B, a prominent member of the BMP family, plays a vital role in orchestrating cellular responses during tissue development and healing. This paper delves into the distinctive features of BMP-8B and presents novel approaches for the production and optimization of BMP-8B human recombinant, aiming to unleash its therapeutic potential in various regenerative contexts.
Characteristics and Signaling Pathways:
BMP-8B is a secreted growth factor belonging to the transforming growth factor-beta (TGF-β) superfamily. It exerts its biological effects by binding to specific cell surface receptors, thereby initiating intricate intracellular signaling cascades. BMP-8B signaling pathways, including Smad-dependent and Smad-independent pathways, regulate crucial processes such as cell differentiation, proliferation, and extracellular matrix synthesis, influencing tissue development and repair.
Production of BMP-8B Human Recombinant:
Efficient production methodologies are essential for harnessing the therapeutic potential of BMP-8B human recombinant. Various recombinant protein expression systems, such as mammalian cells or baculovirus-insect cell systems, have been utilized for the production of functional BMP-8B. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding enhancement, have been employed to improve the yield and bioactivity of BMP-8B recombinant protein.
Potential Therapeutic Applications:
BMP-8B human recombinant holds immense promise in the field of regenerative medicine and tissue engineering. Its involvement in bone and cartilage formation, muscle regeneration, and wound healing makes it a potential candidate for the treatment of skeletal disorders, muscle injuries, and chronic wounds. Furthermore, the ability of BMP-8B to modulate cell behavior and tissue remodeling highlights its broader therapeutic applications in diverse regenerative processes.
Conclusion:
BMP-8B human recombinant emerges as a crucial regulator in regenerative medicine and tissue engineering, offering significant potential for tissue repair and regeneration. Optimizing production methodologies and further unraveling its signaling mechanisms will enhance its therapeutic applications. Given its involvement in bone, cartilage, and muscle formation, as well as wound healing, BMP-8B human recombinant represents a valuable tool for promoting tissue regeneration and addressing the unmet clinical needs in regenerative medicine.
What is the molecular weight/Mw of BMP8B Protein?
BMP8B Protein has a total Mw of 18.1kDa.

What is the source or expression system of BMP8B Protein?
Escherichia Coli.

What is the Purity of BMP8B Protein?
BMP8B Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of BMP8B Protein?
The biological functionality of BMP8B Protein will be determined in the future.

What is the amino acid sequence of BMP8B Protein?
MGSSHHHHHH SSGLVPRGSH MGSAVRPLRR RQPKKSNELP QANRLPGIFD DVHGSHGRQV CRRHELYVSF QDLGWLDWVI APQGYSAYYC EGECSFPLDS CMNATNHAIL QSLVHLMMPD AVPKACCAPT KLSATSVLYY DSSNNVILRK HRNMVVKACG CH.

What applications can BMP8B Protein be used in?
BMP8B Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMP8B Protein?
The endotoxin level is minimal, BMP8B 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 Receptor Type Human Recombinant, His Tag

Tumor necrosis factor receptor superfamily member 1A, Tumor necrosis factor receptor 1, Tumor necrosis factor receptor type I, TNF-R1, TNF-RI, TNFR-I, p60, p55, CD120a, TNFRSF1A, TNFAR, TNFR1, FPF, TBP1, TNF-R, p55-R, TNFR55, TNFR60, TNF-R-I, TNF-R55, MGC19588.

Product # :

CYT-673

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Description

TNFR Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 161 amino acids fragment (41-201) having a molecular weight of 22.68kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The TNFR His Tag is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TNFR His Tag protein is supplied in 1xPBS, 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
TNFR1 belongs to the TNF-receptor superfamily. TNFR1 is a receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha.
There are 2 types of soluble TNF receptors: sTNFR-I and sTNFR-II, which act to neutralize the biological activities of TNF alpha and TNF beta. The levels of these soluble receptors seem to increase as a result of shedding of the extracellular domains of the membrane bound receptors. TNF-a, TNFR1 and TNFR2 have roles in cellular differentiation. TNFR1 and TNFR2 function in cell type-specific renal injury.
TNFR1 is capable of signaling both cell survival and apoptosis. TNFR1-induced apoptosis requires 2 sequential signaling complexes. TNFR1 is capable of activating NF-kappaB, mediate apoptosis, and function as a regulator of inflammation. Oxidative stress promotes TNFR1 and TNFR2 self-interaction, ligand-independent and enhanced ligand-dependent TNF signaling. TNFR1 contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase. Human TNFR1 has a major region which controls cell surface expression. High levels of soluble TNF receptors are found in the amniotic fluid of pregnant women.
Germline mutations of the extracellular domains of TNFR1 are linked to the autosomal dominant periodic fever syndrome. The impaired receptor clearance is believed to be a mechanism of the disease. Familial hibernian fever (FHF) is caused by defects in TNFRSF1A gene.
Synonyms
Tumor necrosis factor receptor superfamily member 1A, Tumor necrosis factor receptor 1, Tumor necrosis factor receptor type I, TNF-R1, TNF-RI, TNFR-I, p60, p55, CD120a, TNFRSF1A, TNFAR, TNFR1, FPF, TBP1, TNF-R, p55-R, TNFR55, TNFR60, TNF-R-I, TNF-R55, MGC19588.
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. Please avoid freeze thaw cycles.
Amino Acid Sequence
DSVCPQGKYIHPQNNSICCTKCHKGTYLYNDCPGPGQ
DTDCRECESGSFTASENHLRHCLSCSKCRKEMGQVE
ISSCTVDRDTVCGCRKNQYRHYWSENLFQCFNCSLCL
NGTVHLSCQEKQNTVCTCHAGFFLRENECVSCSNCKK
SLECTKLCLPQIEN.

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:

B-cell Activating Factor, Mouse Anti Human

BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B.

Product # :

ANT-367

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Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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Introduction
Binds to tnfrsf13b/taci and tnfrsf17/bcma. tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity. A third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response. B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays. Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin.
Synonyms
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B.
Physical Appearance
Sterile Filtered colorless solution.
Immunogen
Anti-human BAFF mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human BAFF amino acids 134-285 purified from E. coli.
Ig Subclass
Mouse IgG3 heavy chain and κ light chain.
Clone
PH4C7AT.
Applications
BAFF antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 1,000. Recommended starting dilution is 1:500.
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
BAFF antibody was purified from mouse ascitic fluids by protein-G 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:

Secretory Leukocyte Peptidase Inhibitor Human Recombinant

Antileukoproteinase, ALK1, ALP, BLPI, HUSI, HUSI-I, MPI, WAP4, WFDC4, WAP four-disulfide core domain protein 4, Protease inhibitor WAP4, Seminal proteinase inhibitor, Mucus proteinase inhibitor.

Product # :

PRO-849

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Description

SLPI Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (26-132 a.a.) and having a molecular mass of 14 kDa. The SLPI is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SLPI Human solution containing 20mM Tris-HCl pH-8.0, 2mM DTT, 0.1M NaCl & 20% glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
SLPI is a secreted inhibitor which guards epithelial tissues from serine proteases. SLPI is localized in various secretions including seminal plasma, cervical mucus, and bronchial secretions, and has affinity for trypsin, leukocyte elastase, and cathepsin G. SLPI inhibitory effect contributes to the immune response by protecting epithelial surfaces from attack by endogenous proteolytic enzymes. SLPI protein has broad-spectrum anti-biotic activity. SLPI is an acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. SLPI prevents elastase-mediated damage to oral and mucosal tissues.
Synonyms
Antileukoproteinase, ALK1, ALP, BLPI, HUSI, HUSI-I, MPI, WAP4, WFDC4, WAP four-disulfide core domain protein 4, Protease inhibitor WAP4, Seminal proteinase inhibitor, Mucus proteinase inhibitor.
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 MSGKSFKAGV CPPKKSAQCL RYKKPECQSD WQCPGKKRCC PDTCGIKCLD PVDTPNPTRR KPGKCPVTYG QCLMLNPPNF CEMDGQCKRD LKCCMGMCGK SCVSPVKA.

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 3K Human Recombinant

Eukaryotic Translation Initiation Factor 3 Subunit K, PLAC-24, eIF3k, eIF-3 p25, eIF-3 p28, EIF3S12, HSPC029, M9, PRO1474, PTD001, Muscle-specific gene M9 protein, ARG134, MSTP001, muscle specific, Eukaryotic Translation Initiation Factor 3 subunit 12.

Product # :

PRO-179

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Description

EIF3K produced in E.Coli is a single, non-glycosylated polypeptide chain containing 238 amino acids (1-218a.a.) and having a molecular mass of 27.2 kDa. EIF3K is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The EIF3K protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
EIF3K is a member of the eIF3 subunit K family. EIF3K is the smallest subunit of eIF3 and it interacts with a number of other subunits of eIF3 and the 40S ribosomal subunit. EIF3K is conserved among high eukaryotes, including mammals, insects, and plants, and it is universally expressed in human tissues. EIF3K is distributed both in nucleus and cytoplasm and colocalized with cyclin D3, a regulatory subunit of cyclin-dependent kinase 4 (Cdk4).
Synonyms
Eukaryotic Translation Initiation Factor 3 Subunit K, PLAC-24, eIF3k, eIF-3 p25, eIF-3 p28, EIF3S12, HSPC029, M9, PRO1474, PTD001, Muscle-specific gene M9 protein, ARG134, MSTP001, muscle specific, Eukaryotic Translation Initiation Factor 3 subunit 12.
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 MAMFEQMRAN VGKLLKGIDR YNPENLATLE RYVETQAKEN AYDLEANLAV LKLYQFNPAF FQTTVTAQIL LKALTNLPHT DFTLCKCMID QAHQEERPIR QILYLGDLLE TCHFQAFWQA LDENMDLLEG ITGFEDSVRK FICHVVGITY QHIDRWLLAE MLGDLSDSQL KVWMSKYGWS ADESGQIFIC SQEESIKPKN IVEKIDFDSV SSIMASSQ

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:

Pigment Epithelium-Derived Factor, Mouse Anti Human

Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

Product # :

ANT-313

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Formulation

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

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Introduction
PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. PEDF is a 50,000 dalton glycoprotein created and secreted in many tissues all the way through the body. A key component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. Additionally, PEDF is capable to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuro-protective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recognition of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities associate it as a potential therapeutic agent for the treatment of vasculature related neurode
Synonyms
Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
Immunogen
Anti-human PEDF mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human PEDF protein 30-504 amino acids purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
Clone
P18E6AT
Applications
PEDF antibody has been tested by ELISA, Western blot analysis and FACS 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.

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-Related Apoptosis Inducing Ligand/Apo2L Mouse Recombinant

Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.

Product # :

CYT-806

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Description

TRAIL Recombinant Mouse produced in E.coli is a single, non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 20.2kDa.

Source

Escherichia Coli.

Formulation

The protein was lyophilized containing PBS, pH 7.4, and 3mM DTT.

Purity

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

Biological Activity

Fully biologically active when compared to standard. The ED50 as determined by a cytotoxicity assay using murine L929 cells is less than 0.5 ng/ml, corresponding to a specific activity of > 2,000,000 IU/mg in the presence of actinomycin D.

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Introduction
TNF-related apoptosis-inducing ligand (TRAIL) is a ligand molecule which induces apoptosis. It is a type II transmembrane protein with homology to other members of the tumor necrosis factor family.In humans, the gene that encodes for TRAIL is located at chromosome 3q26. TRAIL binds to the death receptors, DR4 and DR5. The process of apoptosis is caspase-8-dependent. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues.
Synonyms
Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TRAIL although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TRAIL recombinant 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 TRAIL Mouse Recombinant in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MPRGGRPQKV AAHITGITRR SNSALIPISK DGKTLGQKIE SWESSRKGHS FLNHVLFRNG ELVIEQEGLY YIYSQTYFRF QEAEDASKMV SKDKVRTKQL VQYIYKYTSY PDPIVLMKSA RNSCWSRDAE YGLYSIYQGG LFELKKNDRI FVSVTNEHLM DLDQEASFFG AFLIN

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-gamma Recombinant Rhesus Macaque

Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.

Product # :

CYT-1122

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Description

Interferon-gamma Rhesus Macaque Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 142 amino acid and having a molecular mass of approximately 16.8kDa.IFNG 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 ED50 as determined by an anti-viral assay using human HeLa cells infected with encephalomyocarditis (EMC) virus is < 20.0 ng/ml, corresponding to a specific activity of > 5.0 × 104 IU/mg.

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Introduction
IFN-gamma produced by lymphocytes activated by specific antigens / mitogens.
IFN-gamma, on top of having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons.
Synonyms
Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFNG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Interferon-gamma Rhesus Macaque should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interferon-gamma Rhesus Macaque in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QDPYVKEAEN LKKYFNAGDP DVADNGTLFL DILRNWKEES DRKIMQSQIV SFYFKLFKNF KDDQRIQKSV ETIKEDINVK FFNSNKKKRD DFEKLTNYSV TDSNVQRKAV HELIQVMAEL SPAAKIGKRK RSQMFRGRRA SQ.
Background
What is the molecular weight/Mw of IFNG MONKEY Protein?
IFNG MONKEY Protein has a total Mw of 16.8kDa.

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

What is the Purity of IFNG MONKEY Protein?
IFNG MONKEY Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IFNG MONKEY Protein?
The ED50 as determined by an anti-viral assay using human HeLa cells infected with encephalomyocarditis (EMC) virus is < 20.0 ng/ml, corresponding to a specific activity of > 5.0 × 104 IU/mg.

What is the amino acid sequence of IFNG MONKEY Protein?
QDPYVKEAEN LKKYFNAGDP DVADNGTLFL DILRNWKEES DRKIMQSQIV SFYFKLFKNF KDDQRIQKSV ETIKEDINVK FFNSNKKKRD DFEKLTNYSV TDSNVQRKAV HELIQVMAEL SPAAKIGKRK RSQMFRGRRA SQ.

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

What is the endotoxin level for IFNG MONKEY Protein?
The endotoxin level is minimal, IFNG MONKEY 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:

Interleukin-1 Receptor Antagonist Mouse Recombinant

IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, F630041P17Rik.

Product # :

CYT-658

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Description

IL1 ra Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids and having a molecular mass of 17.4kDa. The IL1ra is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution in water containing NaHCO3.

Purity

Greater than 98.0% as determined by:
(a) Analysis by Gel Filtration.
(b) Analysis by SDS-PAGE.

Biological Activity

The mouse IL-1Ra is capable of inhibiting IL-1-alpha activity in helper T cell line D10.G4.1.

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Introduction
Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.
Synonyms
IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, F630041P17Rik.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin 1ra although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1ra 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-1ra 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 six N-terminal amino acids was determined and was found to be Ala-Cys-Arg-Pro-Ser-Gly.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.91 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).

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:

Fractalkine (CX3CL1) Human Recombinant, Sf9

Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

Product # :

CHM-042

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SDS-PAGE

Description

Fractalkine Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 323 amino acids (25-339aa) and having a molecular mass of 34.3kDa.Fractalkine is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.
Synonyms
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
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
QHHGVTKCNI TCSKMTSKIP VALLIHYQQN QASCGKRAII LETRQHRLFC ADPKEQWVKD
AMQHLDRQAA ALTRNGGTFE KQIGEVKPRT TPAAGGMDES VVLEPEATGE SSSLEPTPSS
QEAQRALGTS PELPTGVTGS SGTRLPPTPK AQDGGPVGTE LFRVPPVSTA ATWQSSAPHQ
PGPSLWAEAK TSEAPSTQDP STQASTASSP APEENAPSEG QRVWGQGQSP RPENSLEREE
MGPVPAHTDA FQDWGPGSMA HVSVVPVSSE GTPSREPVAS GSWTPKAEEP IHATMDPQRL GVLITPVPDA QAATRLEHHH HHH
Background
What is the molecular weight/Mw of CX3CL1 HUMAN, SF9 Protein?
CX3CL1 HUMAN, SF9 Protein has a total Mw of 34.3kDa.

What is the source or expression system of CX3CL1 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of CX3CL1 HUMAN, SF9 Protein?
CX3CL1 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CX3CL1 HUMAN, SF9 Protein?
The biological functionality of CX3CL1 HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of CX3CL1 HUMAN, SF9 Protein?
QHHGVTKCNI TCSKMTSKIP VALLIHYQQN QASCGKRAII LETRQHRLFC ADPKEQWVKD
AMQHLDRQAA ALTRNGGTFE KQIGEVKPRT TPAAGGMDES VVLEPEATGE SSSLEPTPSS
QEAQRALGTS PELPTGVTGS SGTRLPPTPK AQDGGPVGTE LFRVPPVSTA ATWQSSAPHQ
PGPSLWAEAK TSEAPSTQDP STQASTASSP APEENAPSEG QRVWGQGQSP RPENSLEREE
MGPVPAHTDA FQDWGPGSMA HVSVVPVSSE GTPSREPVAS GSWTPKAEEP IHATMDPQRL GVLITPVPDA QAATRLEHHH HHH

What applications can CX3CL1 HUMAN, SF9 Protein be used in?
CX3CL1 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CX3CL1 HUMAN, SF9 Protein?
The endotoxin level is minimal, CX3CL1 HUMAN, SF9 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:

Bone Morphogenetic protein Receptor-1B Human Recombinant

Bone Morphogenetic Protein Receptor, Type IB, BMP Type-1B Receptor, EC 2.7.11.30, BMPR-1B, ALK6, Bone Morphogenetic Protein Receptor Type-1B, Serine/Threonine Receptor Kinase, CDw293 Antigen, EC 2.7.11, CDw293, ALK-6, Bone morphogenetic protein receptor type-1B.

Product # :

CYT-897

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Description

BMPR1B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 136 amino acids (14-126 a.a) and having a molecular mass of 15.1kDa. BMPR1B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BMPR1B protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol, 1mM DTT and 0.1mM PMSF.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Bone Morphogenetic protein Receptor-1B, also known as BMPR1B belongs to the TKL Ser/Thr protein kinase family. BMPR1Bis on ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate as well as activate type I receptors which autophosphorylate, afterward bind and activate SMAD transcriptional regulators. BMPR1B is receptor for BMP7/OP-1 as well as GDF5.
Synonyms
Bone Morphogenetic Protein Receptor, Type IB, BMP Type-1B Receptor, EC 2.7.11.30, BMPR-1B, ALK6, Bone Morphogenetic Protein Receptor Type-1B, Serine/Threonine Receptor Kinase, CDw293 Antigen, EC 2.7.11, CDw293, ALK-6, Bone morphogenetic protein receptor type-1B.
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 MGSKKEDGES TAPTPRPKVL RCKCHHHCPE DSVNNICSTD GYCFTMIEED DSGLPVVTSG CLGLEGSDFQ CRDTPIPHQR RSIECCTERN ECNKDLHPTL PPLKNRDFVD GPIHHR.
Background
Bone Morphogenetic Protein Receptor-1B Human Recombinant: A Key Regulator of Cellular Signaling in Development and Disease
Abstract:
Bone Morphogenetic Protein Receptor-1B (BMPR1B) human recombinant is a critical component of the bone morphogenetic protein (BMP) signaling pathway, governing cellular processes such as embryogenesis, tissue homeostasis, and disease progression. This research paper provides a comprehensive analysis of BMPR1B, including its characteristics, signaling mechanisms, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMPR1B human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine.
Introduction:
The precise regulation of cellular signaling pathways is essential for proper development and tissue maintenance. BMPR1B, a key receptor in the BMP pathway, plays a crucial role in various biological processes. This paper explores the unique features of BMPR1B and presents novel approaches for its production and optimization, aiming to unravel its therapeutic potential in a wide range of developmental and disease contexts.
Characteristics and Signaling Mechanisms:
BMPR1B belongs to the serine/threonine kinase receptor family and is predominantly expressed in embryonic tissues, skeletal structures, and reproductive organs. Upon binding to BMP ligands, BMPR1B initiates downstream signaling cascades, including Smad-dependent and Smad-independent pathways. These pathways regulate gene expression, cellular proliferation, differentiation, and apoptosis, ultimately influencing tissue development and homeostasis.
Production of BMPR1B Human Recombinant:
Efficient production methodologies are pivotal for harnessing the therapeutic potential of BMPR1B human recombinant. Mammalian expression systems, such as Chinese hamster ovary (CHO) cells, have been widely employed to ensure proper folding and post-translational modifications of the receptor. Optimization strategies, including codon optimization and vector engineering, have been utilized to enhance production efficiency. Purification techniques, such as affinity chromatography and size exclusion chromatography, have been optimized to obtain high-quality BMPR1B recombinant protein.
Potential Therapeutic Applications:
BMPR1B human recombinant holds tremendous promise in the field of regenerative medicine and disease therapy. Dysregulation of the BMP signaling pathway has been implicated in various developmental disorders, including skeletal abnormalities and congenital malformations. Modulating BMPR1B activity using BMPR1B human recombinant may offer a targeted approach for promoting tissue regeneration and repair in these conditions. Furthermore, BMPR1B signaling is involved in several diseases, such as cancer and cardiovascular disorders, highlighting its potential as a therapeutic target for intervention.
Conclusion:
BMPR1B human recombinant represents a vital regulator in cellular signaling, with significant implications in development and disease. Optimizing production methodologies and expanding our understanding of its signaling mechanisms will further enhance its therapeutic potential. With its involvement in various biological processes and disease contexts, BMPR1B human recombinant emerges as a promising tool for regenerative medicine and targeted therapeutics.
What is the molecular weight/Mw of BMPR1B Protein?
BMPR1B Protein has a total Mw of 15.1kDa.

What is the source or expression system of BMPR1B Protein?
Escherichia Coli.

What is the Purity of BMPR1B Protein?
BMPR1B Protein is >80% pure as determined by SDS-PAGE.

What is the Biological Activity of BMPR1B Protein?
The biological functionality of BMPR1B Protein will be determined in the future.

What is the amino acid sequence of BMPR1B Protein?
MGSSHHHHHH SSGLVPRGSH MGSKKEDGES TAPTPRPKVL RCKCHHHCPE DSVNNICSTD GYCFTMIEED DSGLPVVTSG CLGLEGSDFQ CRDTPIPHQR RSIECCTERN ECNKDLHPTL PPLKNRDFVD GPIHHR.

What applications can BMPR1B Protein be used in?
BMPR1B Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMPR1B Protein?
The endotoxin level is minimal, BMPR1B 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:

Matrix Metalloproteinase-9 Mouse Recombinant

Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.

Product # :

ENZ-1177

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Description

MMP9 Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 717 amino acids (20-730 a.a.) and having a molecular mass of 79.3 kDa. MMP9 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

MMP9 Mouse protein solution (0.25mg/ml) contains 20mM Tris-HCl pH-7.5, 10mM CaCl2, 100mM NaCl, 0.05% Brij35 and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

Biological Activity

Defined as the amount of enzyme that cleaves 1pmol of Mca-PLGLDpa-AR-NH2 per minute at pH 7.5 at 25C. Specific activity is > 500 pmol/min/ug.

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Introduction
MMP9 is part of the matrix metalloproteinase family. MMP enzymes take part in the dismantle of extracellular matrix in different physiological pathways, for instance wound healing, bone development, reproduction etc. the enzyme is also involved in pathological pathways: metastasis, arthritis and intracerebral hemorrhage.
Synonyms
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.
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
APYQRQPTFV VFPKDLKTSN LTDTQLAEAY LYRYGYTRAA QMMGEKQSLR PALLMLQKQL SLPQTGELDS QTLKAIRTPR CGVPDVGRFQ TFKGLKWDHH NITYWIQNYS EDLPRDMIDD AFARAFAVWG EVAPLTFTRV YGPEADIVIQ FGVAEHGDGY PFDGKDGLLA HAFPPGAGVQ GDAHFDDDEL WSLGKGVVIP TYYGNSNGAP CHFPFTFEGR SYSACTTDGR NDGTPWCSTT ADYDKDGKFG FCPSERLYTE HGNGEGKPCV FPFIFEGRSY SACTTKGRSD GYRWCATTAN YDQDKLYGFC PTRVDATVVG GNSAGELCVF PFVFLGKQYS SCTSDGRRDG RLWCATTSNF DTDKKWGFCP DQGYSLFLVA AHEFGHALGL DHSSVPEALM YPLYSYLEGF PLNKDDIDGI QYLYGRGSKP DPRPPATTTT EPQPTAPPTM CPTIPPTAYP TVGPTVGPTG APSPGPTSSP SPGPTGAPSP GPTAPPTAGS SEASTESLSP ADNPCNVDVF DAIAEIQGAL HFFKDGWYWK FLNHRGSPLQ GPFLTARTWP ALPATLDSAF EDPQTKRVFF FSGRQMWVYT GKTVLGPRSL DKLGLGPEVT HVSGLLPRRL GKALLFSKGR VWRFDLKSQK VDPQSVIRVD KEFSGVPWNS HDIFQYQDKA YFCHGKFFWR VSFQNEVNKV DHEVNQVDDV GYVTYDLLQC P-HHHHHH

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-beta Human Recombinant, Sf9

Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, LT, TNFB, TNFSF1.

Product # :

CYT-989

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Description

Tumor Necrosis Factor-beta Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 180 amino acids (35-205a.a.) and having a molecular mass of 19.7kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).TNFB is fused with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TNFB protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured in a cytotoxicity assay using L-929 mouse fibrosarcoma cells in the presence of the metabolic inhibitor actinomycin D. The ED₅₀ for this effect is ≤ 1ng/ml.

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Introduction
Lymphotoxin alpha, a member of the tumor necrosis factor family, is a cytokine produced by lymphocytes. LTA is highly inducible, secreted, and exists as homotrimeric molecule. LTA forms heterotrimers with lymphotoxin-beta which anchors lymphotoxin-alpha to the cell surface. LTA mediates a large variety of inflammatory, immunostimulatory, and antiviral responses. LTA is also involved in the formation of secondary lymphoid organs during development and plays a role in apoptosis.
Synonyms
Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, LT, TNFB, TNFSF1.
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
ADPLPGVGLT PSAAQTARQH PKMHLAHSTL KPAAHLIGDP SKQNSLLWRA NTDRAFLQDG FSLSNNSLLV PTSGIYFVYS QVVFSGKAYS PKATSSPLYL AHEVQLFSSQ YPFHVPLLSS QKMVYPGLQE PWLHSMYHGA AFQLTQGDQL STHTDGIPHL VLSPSTVFFG AFALHHHHHH.

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:

Myostatin Propeptide Human Recombinant, HEK

GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

Product # :

CYT-936

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Description

Myostatin Propetide Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn24-Arg266) containing a total of 253 amino acids, having a calculated molecular mass of 29.1kDa. Myostatin Propetide is fused to a 10 aa C-terminal His tag.

Source

HEK 293.

Formulation

Myostatin Propetide solution at a concentration of 0.25mg/ml in phosphate buffered saline (PBS) pH 8.0 and 20% (w/v) glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
GDF8 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. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.
Synonyms
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
Physical Appearance
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
NENSEQKENV EKEGLCNACT WRQNTKSSRI EAIKIQILSK LRLETAPNIS KDVIRQLLPK APPLRELIDQ YDVQRDDSSD GSLEDDDYHA TTETIITMPT ESDFLMQVDG KPKCCFFKFS SKIQYNKVVK AQLWIYLRPV ETPTTVFVQI LRLIKPMKDG TRYTGIRSLK LDMNPGTGIW QSIDVKTVLQ NWLKQPESNL GIEIKALDEN GHDLAVTFPG PGEDGLNPFL EVKVTDTPKR SRR HHHHHHH HHH.

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:

TRAIL/APO 2 Ligand (114-281 a.a.) Human Recombinant

Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.

Product # :

CYT-546

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Description

Soluble TNF-related apoptosis-inducing ligand Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (114-281) and having a molecular mass of 19.6 kDa. The sTRAIL is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

1mg/ml in 20mM Tris-HCl pH-7.5, 300mM NaCl, 0.1mM DTT & 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
TNF-related apoptosis-inducing ligand (TRAIL) is a ligand molecule which induces apoptosis. It is a type II transmembrane protein with homology to other members of the tumor necrosis factor family.
In humans, the gene that encodes for TRAIL is located at chromosome 3q26.
TRAIL binds to the death receptors, DR4 and DR5. The process of apoptosis is caspase-8-dependent. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues.
Synonyms
Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.
Physical Appearance
Sterile Filtered colorless liquid.
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
MVRERGPQRV AAHITGTRGR SNTLSSPNSK NEKALGRKIN SWESSRSGHS FLSNLHLRNGELVIHEKGFY YIYSQTYFRF QEEIKENTKN DKQMVQYIYK YTSYPDPILL MKSARNSCWSKDAEYGLYSI YQGGIFELKE NDRIFVSVTN EHLIDMDHEA SFFGAFLVG.

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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