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1000 results found for “Placental Lactogen”
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Name :
PDGFD HumanDescription:
Platelet Derived Growth Factor-D Human Recombinant
Platelet Derived Growth Factor D, Spinal Cord-Derived Growth Factor B, Iris-Expressed Growth Factor, SCDGF-B, IEGF, PDGF-D, MSTP036.
Product # :
CYT-155Price :
Quantity :
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Shipped with Ice Packs
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Description
PDGFD Human Recombinant produced in E. coli is a single polypeptide chain containing 146 amino acids (250-370) and having a molecular mass of 16.6 kDa.PDGFD is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The PDGFD solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Platelet-derived growth factor D (PDGFD) belongs to the platelet-derived growth factor family. PDGFD gene product only forms homodimers and, thus, does not dimerize with the other 3 family members. PDGFD has an imperative role in wound healing. PDGFD induces macrophage recruitment, increased interstitial pressure, and blood vessel maturation during angiogenesis. PDGFD initiates events which lead to a mesangial proliferative glomerulonephritis, including influx of monocytes and macrophages and production of extracellular matrix. The 4 members of the PDGF family are mitogenic factors for cells of mesenchymal origin and are distinguished by a core motif of eight cysteines, 7 of which are found in this factor. PDGFD differs from alpha and beta members of this family by having an odd N-terminal domain, the CUB domain.
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Synonyms
Platelet Derived Growth Factor D, Spinal Cord-Derived Growth Factor B, Iris-Expressed Growth Factor, SCDGF-B, IEGF, PDGF-D, MSTP036.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSYHDR KSKVDLDRLN DDAKRYSCTP RNYSVNIREE LKLANVVFFP RCLLVQRCGG NCGCGTVNWR SCTCNSGKTV KKYHEVLQFE PGHIKRRGRA KTMALVDIQL DHHERCDCIC SSRPPR.
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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Name :
CEACAM8 HumanDescription:
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 8 Human Recombinant
Carcinoembryonic antigen-related cell adhesion molecule 8, CD67 antigen, Carcinoembryonic antigen CGM6, Non-specific cross-reacting antigen NCA-95, CD66b, CGM6, CD67, NCA-95, CEACAM8
Product # :
PRO-2716Price :
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Description
CEACAM8 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 292 amino acids (35-320 a.a) and having a molecular mass of 32.3kDa.CEACAM8 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The CEACAM8 solution (1mg/1ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 8 (CEACAM8) is a cell surface glycoprotein which takes part in cell adhesion in a calciumindependent manner.CEACAM8mediates heterophilic cell adhesion with other carcinoembryonic antigen-related celladhesion molecules (CEACAM6 for example).CEACAM8main role is cell migration,cell adhesion, and pathogen binding.CEACAM-8 isexpressed mainly on the surface of human peripheral blood eosinophils isolated from healthy individuals andused as granulocyte marker.
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Synonyms
Carcinoembryonic antigen-related cell adhesion molecule 8, CD67 antigen, Carcinoembryonic antigen CGM6, Non-specific cross-reacting antigen NCA-95, CD66b, CGM6, CD67, NCA-95, CEACAM8
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
QLTIEAVPSN AAEGKEVLLL VHNLPQDPRG YNWYKGETVD ANRRIIGYVI SNQQITPGPA YSNRETIYPN ASLLMRNVTR NDTGSYTLQV IKLNLMSEEV TGQFSVHPET PKPSISSNNS NPVEDKDAVA FTCEPETQNT TYLWWVNGQS LPVSPRLQLS NGNRTLTLLS VTRNDVGPYE CEIQNPASAN FSDPVTLNVL YGPDAPTISP SDTYYHAGVN LNLSCHAASN PPSQYSWSVN GTFQQYTQKL FIPNITTKNS GSYACHTTNS ATGRNRTTVR MITVSDHHHH HH
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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Name :
Procalcitonin CanineDescription:
Procalcitonin Canine Recombinant
Calcitonin, Calca, Calc, CCALCI.
Product # :
HOR-015Price :
Quantity :
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Shipped at Room temp
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Description
Procalcitonin Canine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Ala26-Arg130) containing 115 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 12.7kDa.
Source
Escherichia Coli.
Formulation
Procalcitonin was filtered (0.4 µm) and lyophilized in 20mM TRIS and 50mM NaCl, pH 7.2.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.
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Synonyms
Calcitonin, Calca, Calc, CCALCI.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Procalcitonin is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHASAPFRSALEGL PDPTALSEKE GRLLLAALVK AYVQRKNELE QEQEQETEGS SLDSSRAKRC SNLSTCVLGT YSKDLNNFHT FSGIGFGAET PGKKRDIASG LERGR.
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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Name :
FSH Human, CHODescription:
Follicle Stimulating Hormone Human Recombinant, CHO
Follitropin subunit beta, Follicle-stimulating hormone beta subunit, FSH-beta, FSH-B, Follitropin beta chain, FSH.
Product # :
HOR-067Price :
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Shipped at Room temp
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Description
FSH Human Recombinant produced in CHO cells is heterodimeric, glycosylated, polypeptide chain transfected with two expression plasmids encoding the human FSH-alpha chain (Accession # P01215) containing 92 amino and human FSH beta chain containing 111 amino acids (Accession # P01225) having a Mw of 33 kDa.
FSH human recombinant is purified by proprietary chromatographic techniques.
Source
CHO Cells
Formulation
The recombinant FSH was lyophilized from 0.2µm filtered solution containing PBS, pH 7.4.
Purity
Greater than 97% by SDS-PAGE and SEC-HPLC analyses.
Biological Activity
Determined by calf testes membrane, binding characteristics to the testicular FSH receptor which was found to be 25 200 pg/mL.More Info
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Introduction
Follicle stimulating hormone (FSH) is a hormone synthesised and secreted by gonadotropes in the anterior pituitary gland. FSH and LH act synergistically in reproduction: In women, in the ovary FSH stimulates the growth of immature Graafian follicles to maturation. As the follicle grows it releases inhibin, which shuts off the FSH production. In men, FSH enhances the production of androgen-binding protein by the Sertoli cells of the testes and is critical for spermatogenesis. In both males and females, FSH stimulates the maturation of germ cells. In females, FSH initiates follicular growth, specifically affecting granulosa cells. With the concomitant rise in inhibin B FSH levels then decline in the late follicular phase. This seems to be critical in selecting only the most advanced follicle to proceed to ovulation. At the end of the luteal phase, there is a slight rise in FSH that seems to be of importance to start the next ovulatory cycle. Like its partner, LH, FSH release at the pituitary gland is controlled by pulses of gonadotropin-releasing hormone (GnRH). Those pulses, in turn, are subject to the estrogen feed-back from the gonads.
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Synonyms
Follitropin subunit beta, Follicle-stimulating hormone beta subunit, FSH-beta, FSH-B, Follitropin beta chain, FSH.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized recombinant FSH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FSH 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.
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Solubility
It is recommended to reconstitute the lyophilized Follicle Stimulating Hormone in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
FSH subunit alpha: APDVQDCPECTLQENPFFSQPGAPILQCMGCCFSRAYPTPLR SKKTMLVQKNVTSESTCCVAKSYNRVTVMGGFKVENHTACHCSTCYYHKS.
FSH subunit beta: NSCELTNITIAIEKEECRFCISINTTWCAGYCYTRDLVYKDP ARPKIQKTCTFKELVYETVRVPGCAHHADSLYTYPVATQCHCGKCDSDSTDCTVRGLGPSYCSFGEMKE.
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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Name :
SGK1 HumanDescription:
Serum/Glucocorticoid Regulated Kinase 1 Human Recombinant
Serine/threonine-protein kinase Sgk1, Serum/glucocorticoid-regulated kinase 1, SGK1, SGK.
Product # :
PKA-272Price :
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Shipped with Ice Packs
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Description
SGK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 393 amino acids (60-431 a.a.) and having a molecular mass of 44.5kDa.SGK1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SGK1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.2M NaCl, 2mM DTT and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Serum-and glucocorticoid-regulated kinase (SGK1) is a serine/threonine protein kinase and a member of the “AGC” subfamily, which includes protein kinases A, G, and C. The SGK1 protein has an imperative role in activating specific potassium, sodium and chloride channels, suggesting a participation in the regulation of processes such as cell survival, neuronal excitability, and renal sodium excretion. SGK1 is activated in vitro by PDK-1 (3-phosphoinositide-dependent protein kinase-1) and in vivo in reaction to signals which activate phosphatidylinositol (PI) 3-kinase.
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Synonyms
Serine/threonine-protein kinase Sgk1, Serum/glucocorticoid-regulated kinase 1, SGK1, SGK.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MISQPQEPEL MNANPSPPPS PSQQINLGPS SNPHAKPSDF HFLKVIGKGS FGKVLLARHK AEEVFYAVKV LQKKAILKKK EEKHIMSERN VLLKNVKHPF LVGLHFSFQT ADKLYFVLDY INGGELFYHL QRERCFLEPR ARFYAAEIAS ALGYLHSLNI VYRDLKPENI LLDSQGHIVL TDFGLCKENI EHNSTTSTFC GTPEYLAPEV LHKQPYDRTV DWWCLGAVLY EMLYGLPPFY SRNTAEMYDN ILNKPLQLKP NITNSARHLL EGLLQKDRTK RLGAKDDFME IKSHVFFSLI NWDDLINKKI TPPFNPNVSG PNDLRHFDPE FTEEPVPNSI GKSPDSVLVT ASVKEAAEAF LGFSYAPPTD SFL.
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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Name :
SPINK1 HumanDescription:
Serine Peptidase Inhibitor Kazal Type 1 Human Recombinant
Serine Peptidase Inhibitor Kazal Type 1, Pancreatic Secretory Trypsin Inhibitor, Tumor-Associated Trypsin Inhibitor, PCTT, TATI, Spink3, Serine Protease Inhibitor Kazal Type 1, TCP, PSTI.
Product # :
ENZ-724Price :
Quantity :
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Shipped with Ice Packs
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Description
SPINK1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 79 amino acids (24-79) and having a molecular mass of 8.6kDa.SPINK1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SPINK1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Trypsin inhibitor SPINK1 is secreted from pancreatic acinar cells into pancreatic fluid. SPINK1 has a role in inhibition of trypsin-catalyzed premature initiation of zymogens in the pancreas and the pancreatic duct. Alterations in SPINK1 gene are the cause for tropical calcific and pancreatitis hereditary pancreatitis.
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Synonyms
Serine Peptidase Inhibitor Kazal Type 1, Pancreatic Secretory Trypsin Inhibitor, Tumor-Associated Trypsin Inhibitor, PCTT, TATI, Spink3, Serine Protease Inhibitor Kazal Type 1, TCP, PSTI.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDSLGREA KCYNELNGCT KIYDPVCGTD GNTYPNECVL CFENRKRQTS ILIQKSGPC.
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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Name :
PKACa2-RIIa2Description:
Protein Kinase A holoenzyme type II alpha Recombinant
Protein Kinase A holoenzyme type II alpha, PKACa2-RIIa2.
Product # :
PKA-205Price :
Quantity :
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Description
Inactive holoenzyme consisting of one dimeric regulatory subunit type II alpha and two monomeric catalytic subunits (cAMP-free). Protein Kinase A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PKA holoenzyme type-II alpha is supplied in 50% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Holoenzyme can be activated by adding the second messenger cAMP (Activation constant about 100nM) releasing two monomeric catalytic subunits.More Info
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Introduction
The protein kinase A holoenzyme is a heterotetramer composed of two types of subunits: Catalytic and Regulatory. The Catalyticsubunit contains the enzyme's active site. It also contains a domain that binds ATP and a domain that binds the regulatory subunit. The Regulatory subunit consists oftwo molecules which bind one another in an anti-parallel orientation to form a homodimer; for type I subunits- this binding is covalent via disulfide bonds. This subunit also has has two domains that bind cyclic AMP, a domain that interacts with a catalytic subunit, and an "auto-inhibitory" domain that serves as a substrate or pseudosubstrate for the catalytic subunit. Regulatory subunits may also have biologic activity distinct from their role in modulating catalytic subunit activity. Regulatory subunits exist in two major forms, RI and RII, with each form having two subtypes designated alpha and beta. Each of the four isotypes of the regulatory subunit is encoded by a different gene. In addition, three isotypes of the catalytic subunit have been identified (alpha, beta and gamma). The different isotypes tend to have different distributions within cells and among tissues. Type I enzymes inhabit cytoplasmic, soluble fractions of the cell, whereas type II enzymes tend to associate with cellular membranes.
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Synonyms
Protein Kinase A holoenzyme type II alpha, PKACa2-RIIa2.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
PKA should be stored at 4°C if entire vial will be used within 2-4 weeks. For long term storage it is recommended to store at -20°C. Avoid multiple freeze-thaw cycles.
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Applications
The product is suitable for analysing PKA type II agonists (cAMP analogs) or antagonists.
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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Name :
LCN2 Human, HisDescription:
Neutrophil Gelatinase Associated Lipocalin/Lipocalin-2 Human Recombinant, His Tag
Neutrophil gelatinase-associated lipocalin, NGAL, p25, 25 kDa alpha-2-microglobulin-related subunit of MMP-9, Lipocalin-2, Oncogene 24p3, LCN2.
Product # :
ENZ-297Price :
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Description
Neutrophil Gelatinase Associated Lipocalin Human Recombinant is expressed in E. coli having a molecular weight of 28.1 kDa fused to an amino terminal hexahistidine tag.The LCN2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lipocalin-2 is supplied in PBS, 50% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Single band on Western Blot.More Info
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Introduction
Recombinant Human Lipocalin-2 also called Neutrophil Gelatinase Associated Lipocalin (NGAL) belongs to a family of lipocans which include 25 proteins (including a1-microglobulin and b-lactoglobulin), which are characterized by their ability to bind small lipophilic substances in their hydrophobic core.
They thereby serve as transporters of substances like retinal, biliverdins & prostaglandins. There are indications that NGAL is involved in modulation of the inflammatory response and is found in the plasma of patients after stroke. -
Synonyms
Neutrophil gelatinase-associated lipocalin, NGAL, p25, 25 kDa alpha-2-microglobulin-related subunit of MMP-9, Lipocalin-2, Oncogene 24p3, LCN2.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. 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.
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Name :
TIMP2 Human HEKDescription:
Tissue Inhibitor of Metalloprotease 2 Human Recombinant, HEK
TIMP metallopeptidase inhibitor 2, CSC-21K, tissue inhibitor of metalloproteinase 2, TIMP-2, metalloproteinase inhibitor 2.
Product # :
ENZ-120Price :
Quantity :
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Shipped at Room temp
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Description
TIMP2 Human Recombinant produced in HEK-293 cells is a secreted protein with the sequence of Human TIMP-2 (amino acids Cys27-Pro220) and is fused to a polyhistidine tag at the C-terminus.
Source
HEK293 Cells.
Formulation
The TIMP2 protein was lyophilized after extensive dialysis against PBS.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The IC50 of 3 nM is measured by its ability to inhibit recombinant human MMP-2 cleavage of the colorimetric peptide substrate, Mca-PLGL-DpaAR-NH2.More Info
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Introduction
TIMP2 belongs to the TIMP gene family. The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases, a group of peptidases that take part in degradation of the extracellular matrix. Besides having an inhibitory role against metalloproteinases, the encoded protein has a exclusive part among TIMPfamily members in its capability to directly suppress the proliferation of endothelial cells. Consequently, the encoded protein is crucial to the conservation of tissue homeostasis by suppressing the production of quiescent tissues as an answer to angiogenic factors, and by inhibiting protease activity in tissues undergoing renovation of the extracellular matrix.
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Synonyms
TIMP metallopeptidase inhibitor 2, CSC-21K, tissue inhibitor of metalloproteinase 2, TIMP-2, metalloproteinase inhibitor 2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TIMP2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TIMP2 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.
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Solubility
It is recommended to reconstitute the lyophilized TIMP2 in sterile assay buffer (50mM Tris, 10mM CaCl2, 150mM NaCl, 0.05% Brij-35, PH 7.5) not less than 100µg/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.
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Name :
CSNK2A2 HumanDescription:
Casein Kinase 2, Alpha 2 Prime Human Recombinant
Casein Kinase 2, Alpha Prime Polypeptide, CK II Alpha, EC 2.7.11.1, CK2A2, EC 2.7.11, CSNK2A1, Casein kinase II subunit alpha'.
Product # :
PKA-042Price :
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Shipped with Ice Packs
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Description
CSNK2A2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 374 amino acids (1-350 a.a) and having a molecular mass of 43.7kDa. CSNK2A2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CSNK2A2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Casein kinase 2 subunit alpha (CSNK2A2) controls numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. CSNK2A2 protein functions as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response.
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Synonyms
Casein Kinase 2, Alpha Prime Polypeptide, CK II Alpha, EC 2.7.11.1, CK2A2, EC 2.7.11, CSNK2A1, Casein kinase II subunit alpha'.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMPGPAA GSRARVYAEV NSLRSREYWD YEAHVPSWGN QDDYQLVRKL GRGKYSEVFE AINITNNERV VVKILKPVKK KKIKREVKIL ENLRGGTNII KLIDTVKDPV SKTPALVFEY INNTDFKQLY QILTDFDIRF YMYELLKALD YCHSKGIMHR DVKPHNVMID HQQKKLRLID WGLAEFYHPA QEYNVRVASR YFKGPELLVD YQMYDYSLDM WSLGCMLASM IFRREPFFHG QDNYDQLVRI AKVLGTEELY GYLKKYHIDL DPHFNDILGQ HSRKRWENFI HSENRHLVSP EALDLLDKLL RYDHQQRLTA KEAMEHPYFY PVVKEQSQPC ADNAVLSSGL TAAR.
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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Name :
HADHB HumanDescription:
2-Enoyl-Coenzyme A (CoA) Hydratase, Beta Human Recombinant
Hydroxyacyl-CoA Dehydrogenase/3-Ketoacyl-CoA Thiolase/Enoyl-CoA Hydratase (Trifunctional Protein) Beta Subunit, Hydroxyacyl-Coenzyme A Dehydrogenase/3-Ketoacyl-Coenzyme A Thiolase/Enoyl-Coenzyme A Hydratase (Trifunctional Protein) Beta Subunit, TP-BETA, 3-Ketoacyl-Coenzyme A (CoA) Thiolase Of Mitochondrial Trifunctional Protein Beta Subunit, 2-Enoyl-Coenzyme A (CoA) Hydratase Beta Subunit, Trifunctional Enzyme Subunit Beta Mitochondrial, Mitochondrial Trifunctional Protein, Acetyl-CoA Acyltransferase, Beta-Ketothiolase, Beta Subunit, EC 2.3.1.16, EC 2.3.1, MSTP029, ECHB, MTPB.
Product # :
ENZ-845Price :
Quantity :
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Shipped with Ice Packs
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Description
HADHB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 464 amino acids (34-474 a.a) and having a molecular mass of 49.9kDa. HADHB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HADHB protein solution (0. 5mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
2-Enoyl-Coenzyme A (CoA) Hydratase, Beta (HADHB) is the beta subunit of the mitochondrial trifunctional protein, that catalyzes the last 3 phases of mitochondrial beta-oxidation of long chain fatty acids. HADHB binds RNA and reduces the stability of various mRNAs. Mutations in HADHB cause trifunctional protein deficiency.
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Synonyms
Hydroxyacyl-CoA Dehydrogenase/3-Ketoacyl-CoA Thiolase/Enoyl-CoA Hydratase (Trifunctional Protein) Beta Subunit, Hydroxyacyl-Coenzyme A Dehydrogenase/3-Ketoacyl-Coenzyme A Thiolase/Enoyl-Coenzyme A Hydratase (Trifunctional Protein) Beta Subunit, TP-BETA, 3-Ketoacyl-Coenzyme A (CoA) Thiolase Of Mitochondrial Trifunctional Protein Beta Subunit, 2-Enoyl-Coenzyme A (CoA) Hydratase Beta Subunit, Trifunctional Enzyme Subunit Beta Mitochondrial, Mitochondrial Trifunctional Protein, Acetyl-CoA Acyltransferase, Beta-Ketothiolase, Beta Subunit, EC 2.3.1.16, EC 2.3.1, MSTP029, ECHB, MTPB.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSAAPAVQT KTKKTLAKPN IRNVVVVDGV RTPFLLSGTS YKDLMPHDLA RAALTGLLHR TSVPKEVVDY IIFGTVIQEV KTSNVAREAA LGAGFSDKTP AHTVTMACIS ANQAMTTGVG LIASGQCDVI VAGGVELMSD VPIRHSRKMR KLMLDLNKAK SMGQRLSLIS KFRFNFLAPE LPAVSEFSTS ETMGHSADRL AAAFAVSRLE QDEYALRSHS LAKKAQDEGL LSDVVPFKVP GKDTVTKDNG IRPSSLEQMA KLKPAFIKPY GTVTAANSSF LTDGASAMLI MAEEKALAMG YKPKAYLRDF MYVSQDPKDQ LLLGPTYATP KVLEKAGLTM NDIDAFEFHE AFSGQILANF KAMDSDWFAE NYMGRKTKVG LPPLEKFNNW GGSLSLGHPF GATGCRLVMA AANRLRKEGG QYGLVAACAA GGQGHAMIVE AYPK.
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.
- View Data Sheet
Name :
MOBKL3 HumanDescription:
MOB1, Mps One Binder kinase Activator-Like 3 Human Recombinant
Mps one binder kinase activator-like 3, 2C4D, Class II mMOB1, Mob1 homolog 3, Mob3, Preimplantation protein 3, MOBKL3, MOB3, PREI3, MOB1, PREI3, CGI-95, MGC12264.
Product # :
PRO-049Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MOBKL3 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 245 amino acids (1-225 a.a.) and having a molecular mass of 28.1kDa. The MOBKL3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MOBKL3 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0) containing 0.2M Nacl, 5mM DTT, 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Mps one binder kinase activator-like 3 (MOBKL3) is a member of the MOB1/Phocein family and is phosphorylated on serine residues. MOBKL3 is usually linked with membranes but can be present in the cytosol, where it behaves as a protein complex. MOBKL3 is the major partner of the striatin family members, which are scaffolding proteins involved in signaling and trafficking.
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Synonyms
Mps one binder kinase activator-like 3, 2C4D, Class II mMOB1, Mob1 homolog 3, Mob3, Preimplantation protein 3, MOBKL3, MOB3, PREI3, MOB1, PREI3, CGI-95, MGC12264.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MVMAEGTAVL RRNRPGTKAQ DFYNWPDESF DEMDSTLAVQ QYIQQNIRAD CSNIDKILEP PEGQDEGVWK YEHLRQFCLE LNGLAVKLQS ECHPDTCTQM TATEQWIFLC AAHKTPKECP AIDYTRHTLD GAACLLNSNK YFPSRVSIKE SSVAKLGSVC RRIYRIFSHA YFHHRQIFDE YENETFLCHR FTKFVMKYNL MSKDNLIVPI LEEEVQNSVS GESEA.
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.
- View Data Sheet
Name :
HOXC11 HumanDescription:
Homeobox C11 Human Recombinant
800x600 Homeobox protein Hox-C11, Homeobox protein Hox-3H, HOXC11, HOX3H.
Product # :
PRO-1658Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
800x600 HOXC11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 327 amino acids (1-304 a.a.) and having a molecular mass of 36.1kDa. HOXC11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HOXC11 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Homeobox C11 (HOXC11) is a member of the Abd-B homeobox family. The homeobox genes encode well conservedfamily of transcription factors that play a vital role in morphogenesis in all multicellular organisms. HOXC11is one of numerous homeobox HOXC genes placed in a cluster on chromosome 12. HOXC11 attaches to a promoterelement of the lactase-phlorizin hydrolase. HOXC11 also takes part in early intestinal development. An alternativelyspliced variant encoding a shorter isoform has been defined however, its full-length nature has not been determined.
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Synonyms
Homeobox protein Hox-C11, Homeobox protein Hox-3H, HOXC11, HOX3H.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMFNSVNL GNFCSPSRKE RGADFGERGS CASNLYLPSC TYYMPEFSTV SSFLPQAPSR QISYPYSAQV PPVREVSYGL EPSGKWHHRN SYSSCYAAAD ELMHRECLPP STVTEILMKN EGSYGGHHHP SAPHATPAGF YSSVNKNSVL PQAFDRFFDN AYCGGGDPPA EPPCSGKGEA KGEPEAPPAS GLASRAEAGA EAEAEEENTN PSSSGSAHSV AKEPAKGAAP NAPRTRKKRC PYSKFQIREL EREFFFNVYI NKEKRLQLSR MLNLTDRQVK IWFQNRRMKE KKLSRDRLQY FSGNPLL.
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.
- View Data Sheet
Name :
HP-NAPDescription:
Neutrophil-activating protein A Helicobacter Pylori Recombinant
DNA protection during starvation protein, Bacterioferritin, HP-NAP, Neutrophil-activating protein A, NAP A, dps, napA.
Product # :
PRO-2035Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
HP-NAP Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Met1-Ala144) containing 154 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 18.2kDa.
Source
Escherichia Coli.
Formulation
HP-NAP was filtered (0.4 µm) and lyophilized in 20mM Tris buffer and 50mM NaCl, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
HP-NAP protects DNA from oxidative damage by sequestering intracellular Fe2+ ion and storing it in the form of Fe3+ oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe2+ ions, thus preventing hydroxyl radical production by the Fenton reaction. HP-NAP is necessary for the survival in the presence of oxidative stress. Dps is also a virulence factor which activates neutrophils, mast cells and monocytes. HP-NAP binds to neutrophil-glycosphingolipids and to sulfated carbohydrates on mucin. HP-NAP might play a part in the accumulation of neutrophils and monocytes at the site of infection. HP-NAP induces superoxide anion generation, adhesion and chemotaxis of neutrophils, via a pertussis toxin-sensitive pathway involving MAP kinases.
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Synonyms
DNA protection during starvation protein, Bacterioferritin, HP-NAP, Neutrophil-activating protein A, NAP A, dps, napA.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. HP-NAP is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHASMKTFEILKHL QADAIVLFMK VHNFHWNVKG TDFFNVHKAT EEIYEEFADM FDDLAERIVQ LGHHPLVTLS EAIKLTRVKE ETKTSFHSKD IFKEILEDYK YLEKEFKELS NTAEKEGDKV TVTYADDQLA KLQKSIWMLQ AHLA.
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.
- View Data Sheet
Name :
EFNA1 Human, HEKDescription:
Ephrin A1 Human Recombinant, HEK
Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.
Product # :
PRO-2477Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
EFNA1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 19-182) containing 170 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 20.2kDa (calculated).
Source
HEK293 cells.
Formulation
EFNA1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline, pH 7.5 containing 5 % (w/v) trehalose.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
EFNA1 belongs to the ephrin (EPH) family. The EPH subfamily is the biggest group of receptor protein kinases and they take part in vital nervous system function and development.
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Synonyms
Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after one week at 4°C.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. EFNA1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
DRHTVFWNSS NPKFRNEDYT IHVQLNDYVD IICPHYEDHS VADAAMEQYI LYLVEHEEYQ LCQPQSKDQV RWQCNRPSAK HGPEKLSEKF QRFTPFTLGK EFKEGHSYYY ISKPIHQHED RCLRLKVTVS GKITHSPQAH DNPQEKRLAA DDPEVRVLHS IGHS 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.
- View Data Sheet
Name :
PDGF BB MouseDescription:
Platelet-Derived Growth Factor BB Mouse Recombinant
Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.
Product # :
CYT-412Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Platelet-Derived Growth Factor BB Mouse Recombinant produced in E.coli, is a homodimeric, non-glycosylated, polypeptide chain containing 2x110 (total of 2 chains 220aa) amino acids and having a total molecular weight of 24.7 kDa.PDGF-BB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from 10mM NaCitrate pH-3.0.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity is determined by the dose-dependant stimulation of the proliferation of human umbelical vein endothelial cells (HUVEC) using a concentration range of less than 1.6ng/ml.More Info
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Introduction
PDGF-BB is a member of the platelet-derived growth factor family. The four members of this family are mitogenic factors for cells of mesenchymal origin and are characterized by a motif of eight cysteines. This gene product can exist either as a homodimer (PDGF-BB) or as a heterodimer with the platelet-derived growth factor alpha polypeptide (PDGF-AB), where the dimers are connected by disulfide bonds. Mutations in this gene are associated with meningioma. Reciprocal translocations between chromosomes 22 and 7, at sites where this gene and that for COL1A1 are located, are associated with a particular type of skin tumor called dermatofibrosarcoma protuberans resulting from unregulated expression of growth factor. Two splice variants have been identified for this gene.
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Synonyms
Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Platelet-derived Growth Factor BB although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF BB 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.
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Solubility
It is recommended to reconstitute the lyophilized Platelet-derived Growth Factor-BB in sterile 100mM acetic acid and 0.1% BSA not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MSLGSLAAAE PAVIAECKTR TEVFQISRNL IDRTNANFLV WPPCVEVQRC SGCCNNRNVQ CRASQVQMRP VQVRKIEIVR KKPIFKKATV TLEDHLACKC ETIVTPRPVT
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Background
Platelet-Derived Growth Factor BB (PDGF-BB) is one of the isoforms of the PDGF family that plays a significant role in embryonic development, cell proliferation, cell migration, and angiogenesis.
It's also relevant in the context of certain pathologies like cancer or healing processes.
Here's what a research paper on Mouse Recombinant PDGF-BB might involve:
Basic Biology:
It might discuss the basic biology and function of PDGF-BB in the mouse model. This could include its role in various cellular processes like cell growth, division, and survival, as well as in the context of tissue repair or angiogenesis.
Recombinant PDGF-BB Production:
The paper might describe methods for producing recombinant PDGF-BB in laboratory conditions. It might go into detail on the expression system used (e.g., bacterial, yeast, or mammalian cells), the purification process, and how the functionality of the produced PDGF-BB was confirmed.
Applications:
It could also detail the experimental applications of recombinant PDGF-BB in the mouse model. For instance, it could be used to study wound healing processes, tissue regeneration, or the development and progression of certain diseases.
Comparative Analysis:
The research might include a comparison of the recombinant PDGF-BB with its natural counterpart in terms of functionality, structure, or other properties.
Innovation:
If the paper is presenting new research, it might discuss an innovative use of PDGF-BB, a novel production method, or new findings about its function.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.48 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of PDGF-BB 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.
- View Data Sheet
Name :
TBCEL HumanDescription:
Tubulin Folding Cofactor E-Like Human Recombinant
Tubulin Folding Cofactor E-Like, E-Like, LRRC351, Leucine Rich Repeat Containing Catastrophin, Tubulin-Specific Chaperone E-Like.
Product # :
PRO-030Price :
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Shipped with Ice Packs
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Description
TBCEL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids and having a molecular mass of 50.6kDa. The TBCEL is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TBCEL solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
TBCEL, is a factor that is in charge of the microtubule cytoskeleton in determining cell behavior. TBCEL plays a role as a regulator of tubulin stability. While widely expressed in testis, TBCEL is also present in several tissues at a much lower level. TBCEL comprises of seven LRR (leucine-rich) repeats, one LRRCT domain and one ubiquitin-like domain. The gene that translates TBCEL consists of 66,704 bases and maps to human chromosome 11q23.3. Chromosome 11 houses over 1,400 genes and consist of nearly 4% of the human genome. Jervell and Lange-Nielsen syndrome, Jacobsen syndrome, Niemann-Pick disease, hereditary angioedema and Smith-Lemli-Opitz syndrome are associated with defects in genes that map to chromosome 11.
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Synonyms
Tubulin Folding Cofactor E-Like, E-Like, LRRC351, Leucine Rich Repeat Containing Catastrophin, Tubulin-Specific Chaperone E-Like.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMDQPSGR SFMQVLCEKY SPENFPYRRG PGMGVHVPAT PQGSPMKDRL NLPSVLVLNS CGITCAGDEK EIAAFCAHVS ELDLSDNKLE DWHEVSKIVS NVPQLEFLNL SSNPLNLSVL ERTCAGSFSG VRKLVLNNSK ASWETVHMIL QELPDLEELF LCLNDYETVS CPSICCHSLK LLHITDNNLQ DWTEIRKLGV MFPSLDTLVL ANNHLNAIEE PDDSLARLFP NLRSISLHKS GLQSWEDIDK LNSFPKLEEV RLLGIPLLQP YTTEERRKLV IARLPSVSKL NGSVVTDGER EDSERFFIRY YVDVPQEEVP FRYHELITKY GKLEPLAEVD LRPQSSAKVE VHFNDQVEEM SIRLDQTVAE LKKQLKTLVQ LPTSNMLLYY FDHEAPFGPE EMKYSSRALH SFGIRDGDKI YVESKTK.
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.
- View Data Sheet
Name :
PNOC HumanDescription:
Prepronociceptin Human Recombinant
Prepronociceptin, Nocistatin, OFQ, Pre-Pro-N/OFQ, Pronociceptin, Orphanin FQ, Nociceptin, PpN/OFQ, N/OFQ, PPNOC.
Product # :
PRO-1442Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PNOC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 180 amino acids (20-176) and having a molecular mass of 20.6kDa. PNOC is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
PNOC protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Prepronociceptin (PNOC) is the ligand of the opioid receptor-like receptor (OPRL1). PNOC functions as a transmitter in the brain by modulating nociceptive and locomotor behavior. The PNOC protein may also be involved in neuronal differentiation and development.
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Synonyms
Prepronociceptin, Nocistatin, OFQ, Pre-Pro-N/OFQ, Pronociceptin, Orphanin FQ, Nociceptin, PpN/OFQ, N/OFQ, PPNOC.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSCQRDCL TCQEKLHPAL DSFDLEVCIL ECEEKVFPSP LWTPCTKVMA RSSWQLSPAA PEHVAAALYQ PRASEMQHLR RMPRVRSLFQ EQEEPEPGME EAGEMEQKQL QKRFGGFTGA RKSARKLANQ KRFSEFMRQY LVLSMQSSQR RRTLHQNGNV.
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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Name :
RLN2 HumanDescription:
Relaxin-2 Human Recombinant
Prorelaxin H2, RLN2, H2, RLXH2, H2-RLX, bA12D24.1.1, bA12D24.1.2.
Product # :
PRO-1327Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RLN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 184 amino acids (25-185 a.a) and having a molecular mass of 20.7kDa.RLN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RLN2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Prorelaxin H2 (RLN2) is a member of a family which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. It may also have other roles in boosting sperm motility, regulating blood pressure, controlling heart rate and releasing vasopressin. RLN2 is a peptide hormone linked to several therapeutically relevant physiological effects, including regulation of collagen metabolism and multiple vascular control pathways. The active form of the RLN2 protein consists of an A chain and a B chain linked by disulfide bonds.
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Synonyms
Prorelaxin H2, RLN2, H2, RLXH2, H2-RLX, bA12D24.1.1, bA12D24.1.2.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDSWMEEV IKLCGRELVR AQIAICGMST WSKRSLSQED APQTPRPVAE IVPSFINKDT ETINMMSEFV ANLPQELKLT LSEMQPALPQ LQQHVPVLKD SSLLFEEFKK LIRNRQSEAA DSSPSELKYL GLDTHSRKKR QLYSALANKC CHVGCTKRSL ARFC.
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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Name :
Vimentin BovineDescription:
Bovine Vimentin
Vimentin, Vim, FLJ36605.
Product # :
PRO-525Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Bovine Vimentin protein produced in Bovine Lens, having a molecular weight of 57 kDa.
Source
Bovine Lens.
Formulation
The protein (1mg/ml) was lyophilized from a 1mg/ml solution containing 10mM sodium phosphate pH 7.5, 6M urea, 2mM DTT, 1mM EDTA and 10mM methylammonium chloride.
Purity
Greater than 98.0% as determined by SDS-PAGE.
More Info
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Introduction
Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines. Vimentin is the main intermediate filament protein in mesenchymal cells and is therefore of value in the differential diagnosis of undifferentiated neoplasms.
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Synonyms
Vimentin, Vim, FLJ36605.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Bovine Vimentin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BovineVimentin 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 Bovine Vimentin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Reconstitution to filaments
After vimentin is dissolved in 6M urea buffer (see above), protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4M urea and then to low salt condition (50mM NaCl, 2mM dithiothreitol, 10mM Sodium Phosphate, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco''s PBS).- Hatzfeld M. and Franke W.W. (1985). J. Cell Biol. 101, 1826-1841.- Hatzfeld M. et al. (1987). J. Mol. Biol. 197, 237-255.
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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Name :
ANGPTL7 HumanDescription:
Angiopoietin-like Protein 7 Human Recombinant
angiopoietin like 7, AngX, CDT6, dJ647M16.1, Angiopoietin-like factor; Angiopoietin-like Protein 7, ANGPTL7, angiopoietinrelated protein 7, Cornea-derived transcript 6 protein
Product # :
CYT-1208Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ANGPTL7 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (27-346a.a) containing 553amino acids and having a molecular mass of 63.2kDa.ANGPTL7 is fused to a 233 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
ANGPTL7 protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Angiopoietin-related protein 7 (ANGPTL7), belongs to the angiopoietin-like family of molecules. ANGPTL7 is expressed in the corneal stroma, trabecular meshwork, and sclera. ANGPTL7 production is up-regulated in trabecular meshwork cells by glucocorticoids and TGF-Beta and in cartilage by TNF-alpha.
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Synonyms
angiopoietin like 7, AngX, CDT6, dJ647M16.1, Angiopoietin-like factor; Angiopoietin-like Protein 7, ANGPTL7, angiopoietinrelated protein 7, Cornea-derived transcript 6 protein
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
QKLSKHKTPA QPQLKAANCC EEVKELKAQV ANLSSLLSEL NKKQERDWVS VVMQVMELES NSKRMESRLT DAESKYSEMN NQIDIMQLQA AQTVTQTSAD AIYDCSSLYQ KNYRISGVYK LPPDDFLGSP ELEVFCDMET SGGGWTIIQR RKSGLVSFYR DWKQYKQGFG SIRGDFWLGN EHIHRLSRQP TRLRVEMEDW EGNLRYAEYS HFVLGNELNS YRLFLGNYTG NVGNDALQYH NNTAFSTKDK DNDNCLDKCA QLRKGGYWYN CCTDSNLNGV YYRLGEHNKH LDGITWYGWH GSTYSLKRVE MKIRPEDFKP LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK
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Background
Angiopoietin-like Protein 7 Human Recombinant: An Emerging Player in Metabolic Regulation and Therapeutic Potential
Abstract:
Angiopoietin-like protein 7 (ANGPTL7) is a multifunctional protein that has recently gained attention for its potential role in metabolic regulation and as a therapeutic target for metabolic disorders. ANGPTL7 is involved in the modulation of lipid metabolism, adipogenesis, and insulin signaling. The availability of human recombinant ANGPTL7 protein has provided researchers with a valuable tool to unravel its biological functions and explore its therapeutic applications. This review provides an overview of the current knowledge on ANGPTL7 and discusses its potential as a therapeutic intervention in metabolic disorders.
Introduction:
Metabolic disorders, including obesity and type 2 diabetes, pose significant health challenges worldwide. ANGPTL7, a member of the angiopoietin-like protein family, has recently emerged as a potential regulator of metabolic processes. ANGPTL7 affects lipid metabolism, adipose tissue biology, and insulin signaling pathways, making it an intriguing target for therapeutic interventions in metabolic disorders.
Role of ANGPTL7 in Metabolic Regulation:
ANGPTL7 plays a multifaceted role in metabolic regulation. It influences lipid metabolism by regulating lipoprotein lipase (LPL) activity and lipid uptake in adipose tissue and skeletal muscle. ANGPTL7 also affects adipocyte biology and adipogenesis, potentially contributing to the development of obesity and related metabolic complications. Furthermore, ANGPTL7 modulates insulin signaling and glucose metabolism, suggesting its involvement in insulin resistance and diabetes pathogenesis.
Mechanisms of ANGPTL7 Action:
ANGPTL7 exerts its effects through various mechanisms. It interacts with extracellular matrix components, influencing cell adhesion and migration. ANGPTL7 also regulates angiogenesis and vascular remodeling, potentially linking it to metabolic regulation and tissue homeostasis.
Therapeutic Potential of ANGPTL7 Human Recombinant Protein:
The availability of ANGPTL7 human recombinant protein offers new avenues for therapeutic interventions in metabolic disorders. Modulating ANGPTL7 activity through recombinant protein administration or targeted interventions may have significant implications for lipid metabolism, adipose tissue function, and insulin sensitivity. Exploring ANGPTL7 as a therapeutic target holds promise for the development of novel strategies to tackle metabolic disorders.
Conclusion:
ANGPTL7 is an emerging player in metabolic regulation with potential therapeutic implications for metabolic disorders. Its involvement in lipid metabolism, adipose tissue biology, and insulin signaling pathways highlights its importance in maintaining metabolic homeostasis. The availability of ANGPTL7 human recombinant protein opens up new possibilities for further investigations and the development of targeted interventions for metabolic disorders.
What is the molecular weight/Mw of ANGPTL7 Protein?
ANGPTL7 Protein has a total Mw of 63.2kDa.
What is the source or expression system of ANGPTL7 Protein?
HEK293 cells.
What is the Purity of ANGPTL7 Protein?
ANGPTL7 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ANGPTL7 Protein?
The biological functionality of ANGPTL7 Protein will be determined in the future.
What is the amino acid sequence of ANGPTL7 Protein?
QKLSKHKTPA QPQLKAANCC EEVKELKAQV ANLSSLLSEL NKKQERDWVS VVMQVMELES NSKRMESRLT DAESKYSEMN NQIDIMQLQA AQTVTQTSAD AIYDCSSLYQ KNYRISGVYK LPPDDFLGSP ELEVFCDMET SGGGWTIIQR RKSGLVSFYR DWKQYKQGFG SIRGDFWLGN EHIHRLSRQP TRLRVEMEDW EGNLRYAEYS HFVLGNELNS YRLFLGNYTG NVGNDALQYH NNTAFSTKDK DNDNCLDKCA QLRKGGYWYN CCTDSNLNGV YYRLGEHNKH LDGITWYGWH GSTYSLKRVE MKIRPEDFKP LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK
What applications can ANGPTL7 Protein be used in?
ANGPTL7 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ANGPTL7 Protein?
The endotoxin level is minimal, ANGPTL7 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
BremelanotideDescription:
Bremelanotide
PT-141, Rekynda, bremelanotide acetate.
Product # :
HOR-039Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
- formulation
- purity
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Description
Bremelanotide Synthetic is a single, non-glycosylated polypeptide chain containing 6 amino acids, having a molecular mass of 1025.16 Dalton and a Molecular formula of C50H68N40O10.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
More Info
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Synonyms
PT-141, Rekynda, bremelanotide acetate.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bremelanotide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Bremelanotide 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.
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Solubility
It is recommended to reconstitute the lyophilized Bremelanotide in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
Ac-Nle-cyclo(-Asp-His-D-Phe-Arg-Trp-Lys)-OH.
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Background
Bremelanotide (PT-141), a synthetic heptapeptide, is a novel therapeutic agent primarily utilized for the treatment of sexual dysfunction. This paper provides an exhaustive review of Bremelanotide, detailing its biochemical structure, mechanism of action, therapeutic applications, and future prospects in clinical medicine.
Bremelanotide (PT-141), derived from Melanotan II, is a synthetic peptide developed for its role in treating sexual dysfunction in both men and women (Clayton et al., 2016). This paper presents a comprehensive examination of Bremelanotide, its biological properties, and potential therapeutic uses.
Bremelanotide acts as a non-selective agonist of the melanocortin receptors, primarily MC3R and MC4R, present in the central nervous system. The peptide initiates its action in the hypothalamus, leading to downstream effects on sexual desire and arousal (King et al., 2007).
The US Food and Drug Administration approved Bremelanotide for the treatment of premenopausal women with hypoactive sexual desire disorder (HSDD) in 2019. In clinical trials, it demonstrated efficacy in enhancing sexual desire and reducing distress associated with HSDD (Kingsberg et al., 2019).
While the current focus of Bremelanotide is on treating sexual dysfunction, its future potential may extend to other areas due to its unique mechanism of action. Further research is needed to explore the full therapeutic potential of this intriguing peptide. In conclusion, Bremelanotide represents a significant advance in sexual dysfunction therapeutics, with potential implications extending beyond this realm.
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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Name :
ProMatrilysinDescription:
ProMatrix Metalloproteinase-7 Recombinant
Product # :
ENZ-272Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28 kDa proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18 kDa active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.
Source
Escherichia Coli.
Formulation
The protein contains the following additives 25mM Tris-HCl (pH 7.5),150mM NaCl, 5mM CaCl2, 0.01% Brij-35 and 0.02% NaN3.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity was found to be 1400 IU/mg.More Info
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Physical Appearance
Sterile clear liquid solution.
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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.
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Unit Definition
One unit is defined as the digestion of 1 µg Azocoll/min at 37°C.
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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Name :
Activin A HumanDescription:
Activin A Human Recombinant
Activin Beta-A chain, Erythroid differentiation protein, EDF, FRP, Activin-A, Inhibin-B, Inihibin-Beta A chain.
Product # :
CYT-569Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
Activin-A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 137 amino acids (311-426) and having a molecular mass of 15.2kDa.Activin-A is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Activin-A protein solution (1mg/ml) contains 20mM Tris pH 8.0 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development. -
Synonyms
Activin Beta-A chain, Erythroid differentiation protein, EDF, FRP, Activin-A, Inhibin-B, Inihibin-Beta A chain.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
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Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 15.2 kDa.What is the source or expression system of Activin A Protein?
E.ColiWhat is the Purity of Activin A Protein?
Activin A Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
The biological functionality of Activin-A Protein will be determined in the future.What is the endotoxin level for Activin A Protein?
The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.What is the amino acid sequence of ACTIVIN A Protein?MGSSHHHHHH SSGLVPRGSH MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS
What applications can ACTIVIN-A Protein be used in?
ACTIVIN A 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.