Search: 1000 results found for "Coagulation Factors"

Description:

RANK Human Recombinant

TNFRSF11A, ODFR, RANK, Tumor Necrosis Factor Receptor Superfamily, Member 11a, Activator Of NFKB, Receptor Activator Of Nuclear Factor-Kappa B, CD265 Antigen, LOH18CR1, TRANCER, CD265

Product # :

CYT-734

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Description

RANK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids and having a molecular mass of 19.1kDa. The RANK is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2 µm filtered concentrated solution in 20mM Tris-HCl, pH 8.0 and 150mM NaCl.

Purity

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

Biological Activity

The ED₅₀ as determined by its ability to inhibit sRANK Ligand induced nuclear factor kappa B (NFkappaB) in RAW 264.7 cells is less than 50 ng/ml, corresponding to a specific activity of
> 2.0 × 10⁴ IU/mg in the presence of 15 ng/ml of recombinant sRANK Ligand.

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Introduction
sRANK Receptor is a part of of the TNF superfamily of ligands and receptors which participates in the regulation of specific immunity and bone turnover. sRANK Receptor was originally acknowledged as a dendritic-cell-membrane protein, which by interacting with RANKL augments the capacity of dendritic cells to stimulate naive T cell proliferation and to endorse the survival of RANK and T cells. The full length human RANK cDNA encodes a type I transmembrane protein of 616 amino acids with a predicted 183 amino acid extracellular domain and a 383 amino acid cytoplasmic domain. sRANK Receptor is also expressed in a various tissues including skeletal muscle, thymus, liver, colon, small intestine and adrenal gland.
Synonyms
TNFRSF11A, ODFR, RANK, Tumor Necrosis Factor Receptor Superfamily, Member 11a, Activator Of NFKB, Receptor Activator Of Nuclear Factor-Kappa B, CD265 Antigen, LOH18CR1, TRANCER, CD265
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized RANK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution sRANK 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 RANK in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QIAPPCTSEK HYEHLGRCCN KCEPGKYMSS KCTTTSDSVC LPCGPDEYLD SWNEEDKCLL HKVCDTGKAL VAVVAGNSTT PRRCACTAGY HWSQDCECCR RNTECAPGLG AQHPLQLNKD TVCKPCLAGY FSDAFSSTDK CRPWTNCTFL GKRVEHHGTE KSDAVCSSSL PARK.

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:

Macrophage Migration Inhibitory Factor Human Recombinant

Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.

Product # :

CYT-575

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Description

Macrophage Inducing Factor Human Recombinant produced in E. coli is a single, non-glycosylated, polypeptide chain containing 115 amino acids (1-115aa) and having a molecular mass of 12kDa. MIF human Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

1mg/ml solution containing 50mM Tris-HCl pH-8, 0.5mM DTT & 10% glycerol.

Purity

Greater than 98.0% as determined by SDS-PAGE.

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Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
Synonyms
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
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
MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFA.

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

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:

Leukemia Inhibitory Factor, GST tag Human Recombinant

D factor, MLPLI, HILDA, Emfilermin, Leukemia Inhibitory factor, Differentiation-stimulating factor, Melanoma-derived LPL inhibitor.

Product # :

CYT-001

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Description

LIF produced in E.Coli is a single, non-glycosylated polypeptide chain containing 415 amino acids (23-202a.a.) and having a molecular mass of 47.2kDa.LIF is fused to a 236 amino acid His-GST tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The LIF GST protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 1mM DTT, 50mM NaCl and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Leukemia inhibitory factor, is a pleiotropic cytokine which is expressed by numerous cells including activated T lymphocytes, monocytes, mast cells and neuronal cells. LIF takes part in the induction of hematopoietic differentiation in normal and myeloid leukemia cells, induction of neuronal cell differentiation, regulator of mesenchymal to epithelial conversion during kidney development, and is a key player in immune tolerance at the maternal-fetal interface.
Synonyms
D factor, MLPLI, HILDA, Emfilermin, Leukemia Inhibitory factor, Differentiation-stimulating factor, Melanoma-derived LPL inhibitor.
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
MHHHHHHMSP ILGYWKIKGL VQPTRLLLEY LEEKYEEHLY ERDEGDKWRN KKFELGLEFP NLPYYIDGDV KLTQSMAIIR YIADKHNMLG GCPKERAEIS MLEGAVLDIR YGVSRIAYSK DFETLKVDFL SKLPEMLKMF EDRLCHKTYL NGDHVTHPDF MLYDALDVVL YMDPMCLDAF PKLVCFKKRI EAIPQIDKYL KSSKYIAWPL QGWQATFGGG DHPPKSDLVP RGSHMSPLPI TPVNATCAIR HPCHNNLMNQ IRSQLAQLNG SANALFILYY TAQGEPFPNN LDKLCGPNVT DFPPFHANGT EKAKLVELYR IVVYLGTSLG NITRDQKILN PSALSLHSKL NATADILRGL LSNVLCRLCS KYHVGHVDVT YGPDTSGKDV FQKKKLGCQL LGKYKQIIAV LAQAF

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:

Platelet-Derived Growth Factor AA Rat Recombinant

Platelet-derived growth factor subunit A, PDGF subunit A, PDGF-1, Platelet-derived growth factor A chain, Platelet-derived growth factor alpha polypeptide, Pdgfa, Rpa1.

Product # :

CYT-776

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Description

Platelet-derived Growth Factor AA Human Recombinant is a disulfide-linked homodimer Consists of two A chains containing 111 amino acids each and having a total molecular mass of 25.3KDa. PDGF-AA is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PDGF-AA was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.0.

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 a cell proliferation assay using murine Balb/c 3T3 cells is less than 5.0 ng/ml, corresponding to a specific activity of > 2.0 × 10⁵ IU/mg.

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Introduction
PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGF is stored in platelet alpha-granules and released upon platelet activation. The PDGF is involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGF
have been identified and named PDGFR-alpha and PDGFR-beta. PDGFR-alpha is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-beta interacts with only PDGF-BB and PDGF-AB.
Synonyms
Platelet-derived growth factor subunit A, PDGF subunit A, PDGF-1, Platelet-derived growth factor A chain, Platelet-derived growth factor alpha polypeptide, Pdgfa, Rpa1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Platelet-derived Growth Factor AA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF-AA 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 Platelet-derived Growth Factor-AA in Sterile 4mM HCl to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.
Amino Acid Sequence
MSIEEAIPAV CKTRTVIYEI PRSQVDPTSA NFLIWPPCVE VKRCTGCCNT SSVKCQPSRV HHRSVKVAKV EYVRKKPKLK EVQVRLEEHL ECACATSNLN PDHREEETDV R.

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:

Activating Transcription Factor-1 Human Recombinant

Activating transcription factor 1, cyclic AMP-dependent transcription factor ATF-1, Protein TREB36, EWS-ATF1, FUS/ATF-1.

Product # :

PKA-019

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Description

ATF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 295 amino acids (1-271 and having a molecular mass of 31.8kDa.ATF1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The ATF1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 5mM DTT, 2mM EDTA and 50% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
ATF1, a cyclic-AMP dependent transcription factor, is expressed in a large selection of cell types and can dimerize with CREB. MSK1 and MSK2 protein kinases are essential for the stress-induced phosphorylation of transcription factors CREB and ATF1 in primary embryonic fibroblasts. Epidermal growth factor induction of c-jun expression needs ATF1 and MEF2 sites in the c-jun promoter.
Synonyms
Activating transcription factor 1, cyclic AMP-dependent transcription factor ATF-1, Protein TREB36, EWS-ATF1, FUS/ATF-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
MGSSHHHHHH SSGLVPRGSH MGSHMEDSHK STTSETAPQP GSAVQGAHIS HIAQQVSSLS ESEESQDSSD SIGSSQKAHG ILARRPSYRK ILKDLSSEDT RGRKGDGENS GVSAAVTSMS VPTPIYQTSS GQYIAIAPNG ALQLASPGTD GVQGLQTLTM TNSGSTQQGT TILQYAQTSD GQQILVPSNQ VVVQTASGDM QTYQIRTTPS ATSLPQTVVM TSPVTLTSQT TKTDDPQLKR EIRLMKNREA ARECRRKKKE YVKCLENRVA VLENQNKTLI EELKTLKDLY SNKSV

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 Human Recombinant, Sf9

Tumor Necrosis Factor, TNFA, Tumor Necrosis Factor Ligand Superfamily Member 2, Cachectin, TNF-Alpha, TNFSF2, TNF-A, Tumor Necrosis Factor (TNF Superfamily, Member 2), Tumor Necrosis Factor-Alpha, TNF, Macrophage-Derived, TNF, Monocyte-Derived, TNF Superfamily, APC1 Protein, Member 2, DIF, Tumor necrosis factor.

Product # :

CYT-903

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Description

TNF a produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 163 amino acids (77-233a.a.) and having a molecular mass of 18.1kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). TNF a is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TNF a protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined bySDS-PAGE.

Biological Activity

Measured in a cytotoxicity assay using L929 mouse fibrosarcoma cells in the presence of the metabolic inhibitor actinomycin D.

The ED50 for this effect is ≤ 0.2 ng/ml.

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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, TNFA, Tumor Necrosis Factor Ligand Superfamily Member 2, Cachectin, TNF-Alpha, TNFSF2, TNF-A, Tumor Necrosis Factor (TNF Superfamily, Member 2), Tumor Necrosis Factor-Alpha, TNF, Macrophage-Derived, TNF, Monocyte-Derived, TNF Superfamily, APC1 Protein, Member 2, DIF, Tumor necrosis factor.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
VRSSSRTPSD KPVAHVVANP QAEGQLQWLN RRANALLANG VELRDNQLVV PSEGLYLIYS QVLFKGQGCP STHVLLTHTI SRIAVSYQTK VNLLSAIKSP CQRETPEGAE AKPWYEPIYL GGVFQLEKGD RLSAEINRPD YLDFAESGQV YFGIIALHHH 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:

Stem Cell Factor Rat Recombinant

Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250, Hematopoietic growth factor KL.

Product # :

CYT-323

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Description

Stem cell factor Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (26-189) and having a molecular mass of 18.4 kDa.The Rat SCF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 0.02% NaHCO3.

Purity

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

Biological Activity

The ED50 is determined by the dose-dependant stimulation of the proliferation of human TF-1 cells which is < 10 ng/ml, corresponding to a specific activity of 100,000units/mg.

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Introduction
Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117 (c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases.
SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid).
Synonyms
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250, Hematopoietic growth factor KL.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized rat SCF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCF 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 SCF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQEICRNPVT DNVKDITKLV ANLPNDYMIT LNYVAGMDVL PSHCWLRDMV THLSVSLTTL LDKFSNISEG LSNYSIIDKL GKIVDDLVAC MEENAPKNVK ESLKKPETRN FTPEEFFSIF NRSIDAFKDF MVASDTSDCV LSSTLGPEKD SRVSVTKPFM LPPVA.

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 / APO2 Ligand 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-443

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Description

TRAIL/APO 2 Ligand Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 168 amino acids (Met+Arg115-Gly281) and having a molecular mass of ~21kDa. The sTRAIL is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a filtered (0.2µm) solution containing 20mM Tris-HCl pH 8.0 and 150mM NaCl.

Purity

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

Biological Activity

The activity is determined by the cytolysis of Murine L929 cells in the presence of Actinomycin D, ED₅₀ for this effect is less than 2ng/ml, corresponding to a specific activity of 5,000,000IU/mg.

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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 APO 2 Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TRAIL 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 TRAIL in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MRERGPQRVA AHITGTRGRS NTLSSPNSKN EKALGRKINS WESSRSGHSF LSNLHLRNGE LVIHEKGFYY IYSQTYFRFQ EEIKENTKND KQMVQYIYKY TSYPDPILLM KSARNSCWSK DAEYGLYSIY QGGIFELKEN DRIFVSVTNE HLIDMDHEAS FFGAFLVG.

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:

Complement Factor H Rat

Complement factor H, H factor 1, CFH, HF, HF1, HF2.

Product # :

PRO-2709

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Description

Rat Complement Factor H produced in Rat plasma having a total molecular mass of 155kDa.

Source

Rat Plasma.

Formulation

CFH protein solution contains phosphate Buffered Saline, pH 7.2.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Complement factor H (CFH) is an important regulatory component of the alternative pathway of complement. CFH is prevents complement activation on host cells and tissues, mainly the kidney. CFH controls the formation and decay of the alternative pathway C3/C5 convertase and acts as a cofactor for factor I which proteolytically inactivates C3b when C3b is bound to factor H. The N-terminal 5 domains of CFH bind to C3b and inhibit binding of factor B thus reducing the formation of C3/C5 convertase. CFH also binds to preformed C3/C5 convertases and causes quick release of the catalytic subunit Bb. These activities are necessary for controlling the spontaneous activation of the alternative pathway amplification process in plasma. In addition, CFH controls the formation and decay of these enzymes when C3b is attached to the surface of particles.
Synonyms
Complement factor H, H factor 1, CFH, HF, HF1, HF2.
Physical Appearance
Sterile filtered solution.
Stability
CFH Rat is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.

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:

Hepatoma-Derived Growth Factor-2 Human Recombinant

Hepatoma-derived growth factor-related protein 3, HRP-3, Hepatoma-derived growth factor 2, HDGF-2, HDGFRP3, HDGF2, CGI-142.

Product # :

CYT-132

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Description

HDGF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (1-203 a.a.) and having a molecular mass of 25.1kDa (Molecular weight on SDS-PAGE will appear higher). HDGF2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HDGF2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

Purity

Greater than 90% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Hepatoma-derived growth factor, related protein 3 (HDGFRP3/HDGF2) is the original member of a family of polypeptides labeled HDGF related proteins (HRPs). The HDGF2 protein augments DNA synthesis and may play a part in cell proliferation. HDGF2 is expressed primarily in the testis and the brain, to an intermediate extent in the heart, and to a slight extent in the ovaries, kidneys, spleen, and liver in humans.
Synonyms
Hepatoma-derived growth factor-related protein 3, HRP-3, Hepatoma-derived growth factor 2, HDGF-2, HDGFRP3, HDGF2, CGI-142.
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 MGSHMARPRP REYKAGDLVF AKMKGYPHWP ARIDELPEGA VKPPANKYPI FFFGTHETAF LGPKDLFPYK EYKDKFGKSN KRKGFNEGLW EIENNPGVKF TGYQAIQQQS SSETEGEGGN TADASSEEEG DRVEEDGKGK RKNEKAGSKR KKSYTSKKSS
KQSRKSPGDE DDKDCKEEEN KSSSEGGDAG NDTRNTTSDL QKTSEGT.
Background
What is the molecular weight/Mw of HDGF2 HUMAN Protein?
HDGF2 HUMAN Protein has a total Mw of 25.1kDa.

What is the source or expression system of HDGF2 HUMAN Protein?
Escherichia Coli.

What is the Purity of HDGF2 HUMAN Protein?
HDGF2 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of HDGF2 HUMAN Protein?
The biological functionality of HDGF2 HUMAN Protein will be determined in the future.

What is the amino acid sequence of HDGF2 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMARPRP REYKAGDLVF AKMKGYPHWP ARIDELPEGA VKPPANKYPI FFFGTHETAF LGPKDLFPYK EYKDKFGKSN KRKGFNEGLW EIENNPGVKF TGYQAIQQQS SSETEGEGGN TADASSEEEG DRVEEDGKGK RKNEKAGSKR KKSYTSKKSS
KQSRKSPGDE DDKDCKEEEN KSSSEGGDAG NDTRNTTSDL QKTSEGT.

What applications can HDGF2 HUMAN Protein be used in?
HDGF2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for HDGF2 HUMAN Protein?
The endotoxin level is minimal, HDGF2 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:

CD70 Human Recombinant, sf9

CD70 Molecule, Tumor Necrosis Factor (Ligand) Superfamily, Member 7, Tumor Necrosis Factor Ligand Superfamily Member 7 , CD27 Ligand, CD27LG, TNFSF7, CD27-L, CD27L, Tumor Necrosis Factor Ligand 8A, Surface Antigen CD70, Ki-24 Antigen, CD70 Antigen, TNLG8A.

Product # :

CYT-953

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Description

TNFSF7 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 164 amino acids (39-193 a.a.) and having a molecular mass of 18.2kDa. TNFSF7 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TNFSF7 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
CD70 also known as TNFSF7 is a cytokine which binds to CD27. TNFSF7 takes part in T-cell activation as well as induces the proliferation of costimulated T-cells. Moreover, TNFSF7 enhances the generation of cytolytic T-cells. Among the diseases which are associated with TNFSF7: Include acute myocarditis & Myocarditis.
Synonyms
CD70 Molecule, Tumor Necrosis Factor (Ligand) Superfamily, Member 7, Tumor Necrosis Factor Ligand Superfamily Member 7 , CD27 Ligand, CD27LG, TNFSF7, CD27-L, CD27L, Tumor Necrosis Factor Ligand 8A, Surface Antigen CD70, Ki-24 Antigen, CD70 Antigen, TNLG8A.
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
ADPQRFAQAQ QQLPLESLGW DVAELQLNHT GPQQDPRLYW QGGPALGRSF LHGPELDKGQ LRIHRDGIYM VHIQVTLAIC SSTTASRHHP TTLAVGICSP ASRSISLLRL SFHQGCTIAS QRLTPLARGD TLCTNLTGTL LPSRNTDETF FGVQWVRPHH HHHH.

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:

Placental Growth Factor-3 Human Recombinant

Placental Growth Factor, Placental Growth Factor Vascular Endothelial Growth Factor-Related Protein, PGFL, PLGF, Placental Growth Factor-Like, Placenta Growth Factor, SHGC-10760, D12S1900, PlGF-2, PGF.

Product # :

CYT-969

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Description

PLGF3 Human Recombinant produced in E.Coli is a non-glycosylated homodimer containing 2x204 amino acids and having a total molecular mass of 45.8kDa.

Source

Escherichia Coli.

Formulation

Lyophilized from a sterile (0.2µm) filtered aqueous solution containing 0.1% Trifluoroacetic Acid (TFA).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
PLGF is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. It binds to receptor vegfr-1/flt1.
Synonyms
Placental Growth Factor, Placental Growth Factor Vascular Endothelial Growth Factor-Related Protein, PGFL, PLGF, Placental Growth Factor-Like, Placenta Growth Factor, SHGC-10760, D12S1900, PlGF-2, PGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PLGF3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PLGF-3 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 PLGF-3 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MLPAVPPQQW ALSAGNGSSE VEVVPFQEVW GRSYCRALER LVDVVSEYPS EVEHMFSPSC VSLLRCTGCC GDENLHCVPV ETANVTMQLL KIRSGDRPSY VELTFSQHVR CECRHSPGRQ SPDMPGDFRA DAPSFLPPRR SLPMLFRMEW GCALTGSQSA VWPSSPVPEE IPRMHPGRNG KKQQRKPLRE KMKPERCGDA VPRR.

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:

Recombinant Human Placental Growth Factor-2, Sf9

PIGF, PGF, PlGF-2, PLGF-2.

Product # :

CYT-420

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Description

Placenta Growth Factor-2 Human Recombinant produced in insect cells is a homodimer, glycosylated polypeptide chain containing 2 x 152 amino acids and having a total molecular mass of 44 kDa. The PLGF-2 is purified by proprietary chromatographic techniques.

Source

Insect Cells.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing BSA.

Purity

Greater than 80.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

PlGF-2 human Recombinant can bind to immobilized rh-sFlt-1 (100ng/well) with a linear range at 0.3–10ng/ml.

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Introduction
PLGF is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. It binds to receptor vegfr-1/flt1.
PLGF-2 binds neuropilin-1 and 2 in a dependent manner.
Synonyms
PIGF, PGF, PlGF-2, PLGF-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Placenta Growth Factor-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PLGF2 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 Placenta Growth Factor 2 in sterile 20mM acetic acid 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:

Hepatoma-Derived Growth Factor (32-285 a.a) Human Recombinant

Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF, DFNB39.

Product # :

CYT-294

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Description

HGF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 255 amino acids (32-285 a.a.) and having a molecular mass of 29.8kDa. HGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 80% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Hepatocyte Growth Factor (HGF) is a multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. HGF synergizes with Interleukin-3 and GM-CSF to stimulate colony formation of hematopoietic progenitor cells in vitro and may, therefore, also modulate hematopoiesis.
Synonyms
Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF, DFNB39.
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
MQRKRRNTIH EFKKSAKTTL IKIDPALKIK TKKVNTADQC ANRCTRNKGL PFTCKAFVFD KARKQCLWFP FNSMSSGVKK EFGHEFDLYE NKDYIRNCII GKGRSYKGTV SITKSGIKCQ PWSSMIPHEH SYRGKDLQEN YCRNPRGEEG GPWCFTSNPE VRYEVCDIPQ CSEVECMTCN GESYRGLMDH TESGKICQRW DHQTPHRHKF LPERYPDKGF DDNYCRNPDG QPRPWCYTLD PHTRWEYCAI KTCET.
Background
What is the molecular weight/Mw of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein has a total Mw of 29.8kDa.

What is the source or expression system of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
Escherichia Coli.

What is the Purity of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein is >80% pure as determined by SDS-PAGE.

What is the Biological Activity of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
What is the molecular weight/Mw of HGF (32-285) HUMAN Protein? HGF (32-285) HUMAN Protein has a total Mw of 29.8kDa. What is the source or expression system of HGF (32-285) HUMAN Protein? Escherichia Coli. What is the Purity of HGF (32-285) HUMAN Protein? HGF (32-285) HUMAN Protein is >80% pure as determined by SDS-PAGE. What is the Biological Activity of HGF (32-285) HUMAN Protein? The biological functionality of HGF (32-285) HUMAN Protein will be determined in the future. What is the amino acid sequence of HGF (32-285) HUMAN Protein? MQRKRRNTIH EFKKSAKTTL IKIDPALKIK TKKVNTADQC ANRCTRNKGL PFTCKAFVFD KARKQCLWFP FNSMSSGVKK EFGHEFDLYE NKDYIRNCII GKGRSYKGTV SITKSGIKCQ PWSSMIPHEH SYRGKDLQEN YCRNPRGEEG GPWCFTSNPE VRYEVCDIPQ CSEVECMTCN GESYRGLMDH TESGKICQRW DHQTPHRHKF LPERYPDKGF DDNYCRNPDG QPRPWCYTLD PHTRWEYCAI KTCET. What applications can HGF (32-285) HUMAN Protein be used in? HGF (32-285) HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow. What is the endotoxin level for HGF (32-285) HUMAN Protein? The endotoxin level is minimal, HGF (32-285) HUMAN Protein was purified using conventional chromatography techniques.

What is the amino acid sequence of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
MQRKRRNTIH EFKKSAKTTL IKIDPALKIK TKKVNTADQC ANRCTRNKGL PFTCKAFVFD KARKQCLWFP FNSMSSGVKK EFGHEFDLYE NKDYIRNCII GKGRSYKGTV SITKSGIKCQ PWSSMIPHEH SYRGKDLQEN YCRNPRGEEG GPWCFTSNPE VRYEVCDIPQ CSEVECMTCN GESYRGLMDH TESGKICQRW DHQTPHRHKF LPERYPDKGF DDNYCRNPDG QPRPWCYTLD PHTRWEYCAI KTCET.

What applications can HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein be used in?
HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
The endotoxin level is minimal, HEPATOCYTE GROWTH FACTOR (32-285) 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 3F Human Recombinant

Eukaryotic Translation Initiation Factor 3, Subunit F, EIF3S5 , Eukaryotic Translation Initiation Factor 3, Subunit 5 (Epsilon, 47kD), EC 3.4.19.12, Deubiquitinating Enzyme EIF3f, eIF3f, eIF-3-epsilon, EIF3 P47, Eukaryotic Translation Initiation Factor 3 Subunit 5, eIF3-p47, Eukaryotic Translation Initiation Factor 3, Subunit 5 Epsilon, 47kDa.

Product # :

PRO-1722

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Description

EIF3F Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 380 amino acids (1-357 a.a) and having a molecular mass of 40kDa. EIF3F is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

EIF3F 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
Eukaryotic Translation Initiation Factor 3F, also known as EIF3F belongs to the eIF-3 subunit F family. EIF3F is a component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which isessential for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosomeand facilitates the recruitment of eIF-1, eIF-1A, eIF 2: GTP: methionyl-tRNAi and eIF-5 to form the 43S preinitiationcomplex (43S PIC). In addition, the eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA forAUG recognition. The eIF-3 complex is also necessary for disassembly and recycling of post termination ribosomalcomplexes and subsequently prevents premature union of the 40S and 60S ribosomal subunits prior to initiation. Among the diseases associated with EIF3F are intrahepatic cholangiocarcinoma, and cholangiocarcinoma.
Synonyms
Eukaryotic Translation Initiation Factor 3, Subunit F, EIF3S5 , Eukaryotic Translation Initiation Factor 3, Subunit 5 (Epsilon, 47kD), EC 3.4.19.12, Deubiquitinating Enzyme EIF3f, eIF3f, eIF-3-epsilon, EIF3 P47, Eukaryotic Translation Initiation Factor 3 Subunit 5, eIF3-p47, Eukaryotic Translation Initiation Factor 3, Subunit 5 Epsilon, 47kDa.
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 MGSMATPAVP VSAPPATPTP VPAAAPASVP APTPAPAAAP VPAAAPASSS DPAAAAAATA APGQTPASAQ APAQTPAPAL PGPALPGPFP GGRVVRLHPV ILASIVDSYE RRNEGAARVI GTLLGTVDKH SVEVTNCFSV PHNESEDEVA VDMEFAKNMY ELHKKVSPNE LILGWYATGH DITEHSVLIH EYYSREAPNP IHLTVDTSLQ NGRMSIKAYV STLMGVPGRT MGVMFTPLTV KYAYYDTERI GVDLIMKTCF SPNRVIGLSS DLQQVGGASA RIQDALSTVL QYAEDVLSGK VSADNTVGRF LMSLVNQVPK IVPDDFETML NSNINDLLMV TYLANLTQSQ IALNEKLVNL.

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 Mouse Recombinant

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

Product # :

CYT-252

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Shipped at Room temp

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Description

Tumor Necrosis Factor-a Mouse Recombinant produced in E. coli is a single, non glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17301.32 Dalton. The TNF-alpha is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.

Purity

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

Biological Activity

The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.1ng/ml, corresponding to a Specific Activity of 10,000,000Units/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
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, 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 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MLRSSSQNSS DKPVAHVVAN HQVEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLVY SQVLFKGQGC PDYVLLTHTV SRFAISYQEK VNLLSAVKSP CPKDTPEGAE LKPWYEPIYL GGVFQLEKGD QLSAEVNLPK YLDFAESGQV YFGVIAL
Background
Tumor Necrosis Factor-alpha (TNF-α) is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. It is primarily produced by activated macrophages, but can also be secreted by other immune cells, such as T cells, natural killer cells, and mast cells. TNF-α is involved in a wide range of physiological and pathological processes, including the defense against infections, the development of autoimmune diseases, and the progression of cancer.
TNF-α exerts its effects by binding to two distinct cell surface receptors, TNF receptor 1 (TNFR1) and TNF receptor 2 (TNFR2). Upon binding to its receptors, TNF-α activates multiple signaling pathways, including the nuclear factor-kappa B (NF-κB) pathway, the mitogen-activated protein kinase (MAPK) pathway, and the apoptotic pathway. These signaling pathways regulate various cellular processes, such as inflammation, cell proliferation, differentiation, and apoptosis.
In the context of infections, TNF-α plays a crucial role in the body's defense against pathogens. It promotes the recruitment and activation of immune cells, enhances the production of other pro-inflammatory cytokines, and stimulates the expression of adhesion molecules on endothelial cells, facilitating the migration of immune cells to the site of infection. TNF-α also helps to induce fever, which is an important component of the body's immune response to infections.
However, excessive or prolonged production of TNF-α can contribute to the development of chronic inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and psoriasis. In these conditions, elevated levels of TNF-α promote the infiltration of immune cells into the affected tissues, leading to tissue damage and the perpetuation of inflammation. The central role of TNF-α in the pathogenesis of these diseases has led to the development of anti-TNF-α therapies, which have revolutionized the treatment of chronic inflammatory diseases. These therapies include monoclonal antibodies, such as infliximab and adalimumab, and soluble TNF receptor fusion proteins, such as etanercept. Anti-TNF-α therapies have been shown to be effective in reducing inflammation, improving symptoms, and slowing disease progression in patients with chronic inflammatory diseases.
In the context of cancer, TNF-α has complex and context-dependent effects on tumor development and progression. On one hand, TNF-α can promote anti-tumor immunity by activating immune cells and stimulating the production of other pro-inflammatory cytokines. On the other hand, chronic inflammation driven by TNF-α can promote tumor growth, angiogenesis, and metastasis. Therefore, the role of TNF-α in cancer is still an area of active research, and the development of TNF-α-targeted therapies for cancer remains a challenge.
In conclusion, TNF-α is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. Its involvement in various physiological and pathological processes has made it an important target for the development of therapies for chronic inflammatory diseases and cancer. Anti-TNF-α therapies have revolutionized the treatment of chronic inflammatory diseases, but the complex role of TNF-α in cancer remains an area of ongoing research. Understanding the precise mechanisms by which TNF-α contributes to disease pathogenesis will be crucial for the development of more effective and targeted therapies.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.24 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 calibrated solution of TNF-a 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:

Vascular Endothelial Growth Factor C Human Recombinant HEK

VEGF-C, Vascular endothelial growth factor C, VRP, Flt4 ligand, Flt4-L, Vascular endothelial growth factor-related protein, VEGFC.

Product # :

CYT-784

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Description

VEGFC Human Recombinant produced by transfected human cells is a single polypeptide chain containing 204 amino acids (32-227). VEGFC is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

VEGFC was lyophilized from a 0.2 µM filtered solution of 20mM Tris-HCl and 150mM NaCl, pH 7.2.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
VEGF-C, also known as Vascular Endothelial Growth Factor Related Protein (VRP), is a recently discovered VEGF growth factor family member that is most closely related to VEGF-D. Human VEGF-C cDNA encodes a pre-pro-protein of 416 amino acids residues. It is almost identical to the mouse VEGF-C protein. Similar to VEGF-D, VEGF-C has a VEGF homology domain spanning the middle third of the precursor molecule and long N- and C-terminal extensions. In adults, VEGF-C is highly expressed in heart, placenta, ovary and small intestine. Recombinant human VEGF-C, lacking the N- and C-terminal extensions and containing only the middle VEGF homology domain, forms primarily non-covalently linked dimers. This protein is a ligand for both VEGFR-2/KDR and VEGFR-3/FLT-4. Since VEGFR-3 is strongly expressed in lymphatic endothelial cells, it has been postulated that VEGF-C is involved in the regulation of the growth and/or differentiation of lymphatic endothelium. Although recombinant human VEGF-C is also a mitogen for vascular endothelial cells, it is much less potent than VEGF-A.
Synonyms
VEGF-C, Vascular endothelial growth factor C, VRP, Flt4 ligand, Flt4-L, Vascular endothelial growth factor-related protein, VEGFC.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized VEGFC although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGFC 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 VEGFC in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
FESGLDLSDAEPDAGEATAYASKDLEEQLRSVSSVDELMTVLYPEYWKMYK
CQLRKGGWQHNREQANLNSRTEETIKFAAAHYNTEILKSIDNEWRKTQCMP
REVCIDVGKEFGVATNTFFKPPCVSVYRCGGCCNSEGQCMNTSTSYLSKTLF
EITVPLSQGPKPVTISFANHTSCRCMSKLDVYRQVHSIIRRVDHHHHHH.

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:

Platelet-Derived Growth Factor Receptor, Alpha Human Recombinant

Platelet-derived growth factor receptor alpha polypeptide, PDGFR2, PDGF-R-alpha, CD140 antigen-like family member A, CD140a antigen, alpha-type platelet-derived growth factor receptor, RHEPDGFRA, rearranged-in-hypereosinophilia-platelet derived growth factor receptor alpha, PDGFRA/BCR fusion protein, MGC74795, EC 2.7.10.1.

Product # :

CYT-065

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Description

PDGFRA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 522 amino acids (24-524) and having a molecular mass of 58.4 kDa.The PDGFRA is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The PDGFRA solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 20% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
PDGFRa is a cell surface tyrosine kinase receptor for PDGF family members. PDGFRa binds to both A and B subunits of PDGF. It is known that PDGFRa is vital for kidney development since mice heterozygous for the receptor display defective kidney phenotypes.
Synonyms
Platelet-derived growth factor receptor alpha polypeptide, PDGFR2, PDGF-R-alpha, CD140 antigen-like family member A, CD140a antigen, alpha-type platelet-derived growth factor receptor, RHEPDGFRA, rearranged-in-hypereosinophilia-platelet derived growth factor receptor alpha, PDGFRA/BCR fusion protein, MGC74795, EC 2.7.10.1.
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
MGSSHHHHHH SSGLVPRGSH MQLSLPSILP NENEKVVQLN SSFSLRCFGE SEVSWQYPMS EEESSDVEIR NEENNSGLFV TVLEVSSASA AHTGLYTCYY NHTQTEENEL EGRHIYIYVP DPDVAFVPLG MTDYLVIVED DDSAIIPCRT TDPETPVTLH NSEGVVPASY DSRQGFNGTF TVGPYICEAT VKGKKFQTIP FNVYALKATS ELDLEMEALK TVYKSGETIV VTCAVFNNEV VDLQWTYPGE VKGKGITMLE EIKVPSIKLV YTLTVPEATV KDSGDYECAA RQATREVKEM KKVTISVHEK GFIEIKPTFS QLEAVNLHEV KHFVVEVRAY PPPRISWLKN NLTLIENLTE ITTDVEKIQE IRYRSKLKLI RAKEEDSGHY TIVAQNEDAV KSYTFELLTQ VPSSILDLVD DHHGSTGGQT VRCTAEGTPL PDIEWMICKD IKKCNNETSW TILANNVSNI ITEIHSRDRS TVEGRVTFAK VEETIAVRCL AKNLLGAENR ELKLVAPTLR SE.

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:

DNA Fragmentation Factor Subunit Alpha Human Recombinant

DNA fragmentation factor subunit alpha, DNA fragmentation factor 45 kDa subunit, DFF-45, Inhibitor of CAD, ICAD, DFFA, DFF1, DFF45.

Product # :

PRO-718

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Description

DFFA Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 351 amino acids (1- 331 a.a.) and having a molecular mass of 38.7kDa.The DFFA is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The DFFA solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
DFF is a heterodimeric protein of 40kDa (DFFB) and 45kDa (DFFA) subunits. DFFA (DNA fragmentation factor subunit alpha) is the substrate for caspase-3 and triggers DNA fragmentation during apoptosis. DFF is activated once DFFA is cleaved by caspase-3. The cleaved fragments of DFFA detach from DFFB (the active component of DFF), which in turn triggers DNA fragmentation as well as chromatin condensation during apoptosis. Apoptosis is accompanied by shrinkage and fragmentation of the cells and nuclei and degradation of the chromosomal DNA into nucleosomal units.
A reduced level of DFFA detected in ovarian endometriosis may be a part of an apoptosis-resistant mechanism enhancing the disease progression.
DFFA at chromosome 1 shows rare allelic variants in neuroblastoma tumors.
Synonyms
DNA fragmentation factor subunit alpha, DNA fragmentation factor 45 kDa subunit, DFF-45, Inhibitor of CAD, ICAD, DFFA, DFF1, DFF45.
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 MEVTGDAGVP ESGEIRTLKP CLLRRNYSRE QHGVAASCLE DLRSKACDIL AIDKSLTPVT LVLAEDGTIV DDDDYFLCLP SNTKFVALAS NEKWAYNNSD GGTAWISQES FDVDETDSGA GLKWKNVARQ LKEDLSSIIL LSEEDLQMLV DAPCSDLAQE LRQSCATVQR LQHTLQQVLD QREEVRQSKQ LLQLYLQALE KEGSLLSKQE ESKAAFGEEV DAVDTGISRE TSSDVALASH ILTALREKQA PELSLSSQDL ELVTKEDPKA LAVALNWDIK KTETVQEACE WELALRLQQT QSLHSLRSIS ASKASPPGDL QNPKRARQDP T.

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:

Placental Growth Factor-2 Human Recombinant, CHO

PIGF, PGF, PlGF-2, PLGF-2.

Product # :

CYT-868

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Description

PLGF2 Human Recombinant (19-170 a.a.) produced in CHO is a disulfide-linked homodimeric, glycosylated, polypeptide chain containing 152 amino acids and having a molecular mass of 33kDa.The PLGF-2 Human Recombinant protein is purified by proprietary chromatographic techniques.

Source

Chinese Hamster Ovary cells (CHO).

Formulation

PLGF-2 protein was lyophilized from a 0.2µm filtered solution in HCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as measured in a cell proliferation assay using MDA?MB?231 cells is less than 10µg/ml.

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Introduction
PLGF is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. It binds to receptor vegfr-1/flt1.
PLGF-2 binds neuropilin-1 and 2 in a heparin-dependent manner.
Synonyms
PIGF, PGF, PlGF-2, PLGF-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PLGF-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PLGF2 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 PLGF2 at 200µg/ml in PBS, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
LPAVPPQQWA LSAGNGSSEV EVVPFQEVWG RSYCRALERL VDVVSEYPSE VEHMFSPSCV SLLRCTGCCG DENLHCVPVE TANVTMQLLK IRSGDRPSYV ELTFSQHVRC ECRPLREKMK PERRRPKGRG KRRREKQRPT DCHLCGDAVP RR.

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:

Placental Growth Factor-1 Human Recombinant

PIGF, PGF, PLGF-1.

Product # :

CYT-1227

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Description

PLGF1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 19-149) containing 137 amino acids and having a molecular mass of 15.5kDa. PLGF1 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

PLGF1 protein (0.5mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured by its binding ability in a functional ELISA with Human VEGFR1/Flt-1.

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Synonyms
PIGF, PGF, PLGF-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
LPAVPPQQWA LSAGNGSSEV EVVPFQEVWG RSYCRALERL VDVVSEYPSE VEHMFSPSCV SLLRCTGCCG DENLHCVPVE TANVTMQLLK IRSGDRPSYV ELTFSQHVRC ECRPLREKMK PERCGDAVPR RHHHHHH.
Background
Implications in Pathological Angiogenesis:
While PLGF1 is essential for normal vascular development, dysregulation of its expression is associated with pathological angiogenesis. In conditions such as cancer, PLGF1 can contribute to the formation of abnormal blood vessels that support tumor growth and metastasis. Investigations involving PLGF1 Human Recombinant provide insights into the mechanisms by which PLGF1 contributes to pathological angiogenesis, offering potential targets for anti-angiogenic therapies.
Challenges and Future Directions:
While the potential of PLGF1 Human Recombinant in understanding angiogenesis is evident, challenges persist. Fine-tuning its applications, understanding its interactions with other angiogenic factors, and deciphering the context-dependent nature of its functions are critical considerations for translational success. Additionally, developing strategies to selectively target PLGF1 in pathological conditions without compromising its physiological roles poses a challenge in the pursuit of therapeutic interventions.
PLGF1 Human Recombinant stands at the forefront of angiogenesis research, offering a controlled platform for scientific exploration. Its structural insights, angiogenic signaling functions, and implications in both physiological and pathological contexts position it as a key player in the evolving landscape of vascular biology. As researchers continue to delve into the molecular intricacies of PLGF1, they not only enhance our understanding of angiogenesis but also pave the way for transformative advancements in vascular-targeted therapies, shaping the future of precision medicine and anti-angiogenic interventions.

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:

Human Thrombin

Product # :

PRO-339

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Description

Thrombin was purified from human plasma.

Source

Human Plasma.

Formulation

Lyophilized protein containing mannitol, sodium chloride, calcium chloride.

Biological Activity

The specific activity was found to be 116 US Units/mg protein.

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Introduction
Thrombin enzyme (Activated Factor IIa) is an important clotting promoter that controls the transformation of soluble fibrinogen to insoluble active fibrin strands. Thrombin is a coagulation protein and a serine protease (EC 3.4.21.5) that catalyzes many coagulation-related reactions. Thrombin triggers factor-XI, factor-V, Factor-XIII and factor-VIII. Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet. As a result of its high proteolytic specificity, thrombin has become an important biochemical protein. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is widely used in linker regions of recombinant fusion protein constructs. After the purification of the fusion protein, thrombin is used to cleave between the Arginine and Glycine residues of the cleavage site, efficiently removing the purification tag from the protein of interest with a high degree of specificity.
Physical Appearance
lyophilized powder.
Stability
Lyophilized Human Thrombin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution human thrombin 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 human thrombin in sterile a 0.9% NaCl solution at 500U/ml.

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:

Complement C1q Tumor Necrosis Factor-Related Protein 5 Human Recombinant

CTRP5, MFRP.

Product # :

PRO-2599

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Description

C1QTNF5 Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 253 amino acids (16-243.a.a) and having a molecular mass of 26.4kDa. C1QTNF5 Human is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The C1QTNF5 protein solution (0.25 mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.5) containing 30% glycerol and 0.2M NaCl.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Complement C1q Tumor Necrosis Factor-Related Protein 5 (C1QTNF5) encodes a short-chain collagen which is expressed mainly in sub-retinal pigment epithelium, ciliary epithelium and adipose tissue. C1QTNF5 is increased in mtDNA-depleted myocytes and stimulates the phosphorylation of AMP activated protein kinase. C1QTNF5 takespart in the adhesion of the retinal pigment epithelium (RPE) to the Bruch Membrane. Mutations in C1QTNF5 have been associated with late-onset retinal degeneration.
Synonyms
CTRP5, MFRP.
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 MGSHMSPPLD DNKIPSLCPG HPGLPGTPGH HGSQGLPGRD
GRDGRDGAPG APGEKGEGGR PGLPGPRGDP GPRGEAGPAG PTGPAGECSV PPRSAFSAKR
SESRVPPPSD APLPFDRVLV NEQGHYDAVT GKFTCQVPGV YYFAVHATVY RASLQFDLVK
NGESIASFFQ FFGGWPKPAS LSGGAMVRLE PEDQVWVQVG VGDYIGIYAS IKTDSTFSGF LVYSDWHSSP VFA.

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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