Search results
1000 results found for “ephrin”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
BuserelinDescription:
Buserelin
Product # :
HOR-255Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
Description
Buserelin contains 9 amino acids Glu-His-Trp-Ser-Tyr-D-Ser(tBu)-Leu-Arg-Pro-NHEt and having a molecular weight of 1239.44 Dalton.
Formulation
The Buserelin peptide was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Buserelin belongs to the group of gonadotrophin releasing hormone (gonadorelin) analogues (LHRH agonist). It acts on the pituitary gland which controls the amount of many different types of hormones (chemical messengers). It alters the amount of hormones, particularly the oestrogens androgens. This alteration of hormone levels can be exploited to treat cancers of the prostate gland, which are stimulated to grow by testosterone. Buserelin lowers the levels of testosterone, which starves the tumour of testosterone and causes it to shrink.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Buserelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Buserelin 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 Buserelin in sterile 18MΩ-cm H2O not less than 100 µg/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.
- View Data Sheet
Name :
ACVR1 HumanDescription:
Activin A Receptor Type 1 Human Recombinant
ACVR1A, ALK2, ACVR1, ACTRI, ACTR-I, ACVRLK2, FOP, SKR1, TSRI, Activin receptor type I, Activin receptor-like kinase 2, ALK-2, TSR-I, Serine/threonine-protein kinase receptor R1, TGF-B superfamily receptor type I.
Product # :
CYT-1140Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- sds-page
Description
ACVR1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 342 amino acids (21-123a.a.) and having a molecular mass of 38.4kDa. ACVR1 is expressed with a 239 amino acid hIgG-His-Tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ACVR1 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.
sds-page
More Info
-
Introduction
Activin A Receptor Type 1 (ACVR1) is a member of TGF-beta serine/threonine kinase receptor family. ACVR1 forms a receptor complex contains2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate,bind and activate SMAD transcriptional regulators. ACVR1 takes part in left-right pattern formation during embryogenesis and is also essential in the BMP pathway which is responsible for the development and repair of the skeletal system.ACVR1 is linked to Fibrodysplasia Ossificans Progressiva which isknown for the formation of heterotopic bone throughout the body.
-
Synonyms
ACVR1A, ALK2, ACVR1, ACTRI, ACTR-I, ACVRLK2, FOP, SKR1, TSRI, Activin receptor type I, Activin receptor-like kinase 2, ALK-2, TSR-I, Serine/threonine-protein kinase receptor R1, TGF-B superfamily receptor type I.
-
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
MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN DGFHVYQKGC FQVYEQGKMT
CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF HLELEPKSCD KTHTCPPCPA
PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP
REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL
PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT
VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH. -
Background
Functional Implications and Therapeutic Prospects of Activin A Receptor Type 1 Human Recombinant
1. Abstract
This study illuminates the functional roles and potential therapeutic applications of Activin A Receptor Type 1 Human Recombinant (ACVR1), a crucial protein in the TGF-beta superfamily signaling pathway. Through a comprehensive review of its structure, signaling mechanism, biological functions, and disease associations, this paper aims to elucidate the current understanding of ACVR1 and its potential therapeutic implications in various disease states.
2. Introduction
The Activin A Receptor Type 1 Human Recombinant, abbreviated as ACVR1, is a receptor protein vital for transmitting cellular signals in the Transforming Growth Factor-beta (TGF-beta) superfamily pathway. Known to play pivotal roles in organogenesis, bone growth, and cell differentiation, the ACVR1 and its functions present vast therapeutic potential.
3. Structure and Signaling of ACVR1
ACVR1 is a transmembrane serine/threonine kinase receptor, characterized by an extracellular ligand-binding domain and an intracellular kinase domain for signal transduction. Binding of ligands such as Activin A leads to the formation of heteromeric complexes with type II receptors, triggering phosphorylation events that activate downstream signaling pathways.
4. Biological Functions of ACVR1
Being a part of the TGF-beta superfamily signaling pathway, ACVR1 is implicated in a broad spectrum of biological processes. It is crucial for embryonic development, cellular proliferation, differentiation, apoptosis, and homeostasis. It also plays a significant role in bone morphogenesis, contributing to skeletal patterning and growth.
5. ACVR1 in Disease Pathology
The dysregulation of ACVR1 has been associated with various pathological conditions, including Fibrodysplasia Ossificans Progressiva (FOP), a rare genetic disorder characterized by progressive ossification of soft tissues. Mutations in ACVR1 lead to enhanced BMP signaling, causing aberrant bone formation. This highlights the critical role of ACVR1 in skeletal homeostasis and disease.
6. Therapeutic Potential of ACVR1
Given the central role of ACVR1 in cellular signaling and its association with disease, it presents a promising target for therapeutic intervention. Strategies to modulate ACVR1 signaling could potentially ameliorate symptoms of diseases like FOP, offering promising avenues for novel therapeutic approaches.
7. Conclusion and Future Perspectives
While our understanding of ACVR1's functional roles has expanded significantly over the years, much remains to be elucidated. Further research into the precise molecular mechanisms of ACVR1 and its pathway will pave the way for therapeutic advances, enhancing our capability to combat various diseases.
What is the molecular weight / Mw of ACVR1 Protein?
ACVR1 Protein has a total Mw of 38.4kDa.
What is the source or expression system of ACVR1 Protein?
Sf9, Baculovirus cells.
What is the Purity of ACVR1 Protein?
ACVR1 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ACVR1 Protein?
The biological functionality of ACVR1 Protein will be determined in the future.
What is the endotoxin level for ACVR1 Protein?
The endotoxin level is minimal, ACVR1 Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of ACVR1 Protein?
MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN DGFHVYQKGC FQVYEQGKMT
CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF HLELEPKSCD KTHTCPPCPA
PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP
REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL
PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT
VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.
What applications can ACVR1 Protein be used in?
ACVR1 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.
- View Data Sheet
Name :
EEF1B2 HumanDescription:
Eukaryotic Translation Elongation Factor 1 Beta 2 Human Recombinant
Elongation factor 1-beta, EF-1-beta, EEF1B2, EEF1B, EF1B, EEF1B1.
Product # :
PRO-167Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
EEF1B2 Human Recombinant fused with an 8 amino acid His tag at C-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 233 amino acids (1-225 a.a.) and having a molecular mass of 25.8kDa. The EEF1B2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EEF1B2 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 100mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Elongation factor 1-beta (EEF1B2) is a translation elongation factor. EEF1B2 is a guanine nucleotide exchange factor which is involved in the transfer of aminoacylated tRNAs to the ribosome. Both EEF1B2 and EEF1D stimulate the exchange of GDP bound to EEF1A to GTP.
-
Synonyms
Elongation factor 1-beta, EF-1-beta, EEF1B2, EEF1B, EF1B, EEF1B1.
-
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
MGFGDLKSPA GLQVLNDYLA DKSYIEGYVP SQADVAVFEA VSSPPPADLC HALRWYNHIK SYEKEKASLP GVKKALGKYG PADVEDTTGS GATDSKDDDD IDLFGSDDEE ESEEAKRLRE ERLAQYESKK AKKPALVAKS SILLDVKPWD DETDMAKLEE CVRSIQADGL VWGSSKLVPV GYGIKKLQIQ CVVEDDKVGT DMLEEQITAF EDYVQSMDVA AFNKILEHHH 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.
- View Data Sheet
Name :
EGF AntibodyDescription:
Endothelial Growth Factor, Mouse Anti-Human
Urogastrone, URG, EGF.
Product # :
ANT-169Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- formulation
- More Info
Formulation
1mg/ml in PBS (after reconstitution).
More Info
-
Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. -
Synonyms
Urogastrone, URG, EGF.
-
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
-
Immunogen
r.HumanEGF.
-
Ig Subclass
Mouse IgG2b.
-
Clone
NYRhEGF.
-
Applications
Direct ELISA, Western Blot, Immuneprecipitation.
-
Titer
By direct ELISA, 1:10,000 dilution will yield 0.3 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
-
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
-
Type
Mouse Anti Human Monoclonal.
-
Storage Procedures
In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
-
Purification Method
Ion exchange.
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 :
Fibronectin RatDescription:
Fibronectin Rat
Product # :
PRO-131Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Plasma fibronectin level is elevated in severe coronary artery disease. Increased plasma fibronectin levels are related with venous thromboembolism (VTE) particularly in males, and extend the probable association between biomarkers and risk factors for arterial atherothrombosis and VTE. Fibronectin plays a role in several cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion. Fibronectin consists in two main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the etracellular matrix and 2) as a soluble disulphide linked dimer found in the plasma. The plasma form is produced by hepatocytes, and the ECM form is synthesized by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin alos takes part as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates. Fibronectin organizes cellular interaction with the ECM by binding to different components of the extracellular matrix and to membrane-bound Fibronectin receptors on cell surfaces. Molecular Weight 220kDa.
Source
Rat Plasma.
Formulation
The Rat Fibronectin was lyophilized from a concentrated 1mg/ml solution containing 20mM Tris Cl pH-7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store the lyophilized fibronectin at 4°C. Upon reconstitution fibronectin should be stored at 4°C for 2 weeks and for future use below -18°C.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Rat Fibronectin in sterile 18M-cm H2O 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.
- View Data Sheet
Name :
Follistatin HumanDescription:
Follistatin Human Recombinant
FST, FS
Product # :
CYT-232Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Follistatin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids and having a total molecular mass of 31.5kDa.The FST is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing no additives.
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 ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.
More Info
-
Introduction
Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin functions as an ACTV antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).
-
Synonyms
FST, FS
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Follistatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FST 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 Follistatin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Asn-Cys-Trp-Leu.
-
Background
What is the molecular weight/Mw of FOLLISTATIN HUMAN Protein?
FOLLISTATIN HUMAN Protein has a total Mw of 31.5kDa.
What is the source or expression system of FOLLISTATIN HUMAN Protein?
Escherichia Coli.
What is the Purity of FOLLISTATIN HUMAN Protein?
FOLLISTATIN HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FOLLISTATIN HUMAN Protein?
The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.
What is the amino acid sequence of FOLLISTATIN HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Asn-Cys-Trp-Leu.
What applications can FOLLISTATIN HUMAN Protein be used in?
FOLLISTATIN HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FOLLISTATIN HUMAN Protein?
The endotoxin level is minimal, FOLLISTATIN 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.
- View Data Sheet
Name :
Adiponectin Human, HMWDescription:
Adiponectin glycosylated Human Recombinant, HMW Rich
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-764Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Adiponectin Human Recombinant HMW Rich produced in HEK cells is a single, glycosylated, polypeptide chain (19-244) containing a total of 226 amino acids, having a molecular mass of 24.6kDa (calculated). Human Acrp30 HMW Rich migrates on SDS-PAGE under non-reducing conditions at ~ 884 kDa.
Source
HEK293.
Formulation
Acrp30 was filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris, 50mM NaCl, pH 7.5 and 1mM CaCl2.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.
-
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
-
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.
-
Solubility
It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Acrp30 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHITVYM KDVKVSLFKK DKAMLFTYDQ YQENNVDQAS GSVLLHLEVG DQVWLQVYGE GERNGLYADN DNDSTFTGFL LYHDTN.
-
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 24.6 kDa.
What is the source or expression system of ADIPONECTIN Protein?
HEK293.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What is the amino acid sequence of ADIPONECTIN Protein?
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHITVYM KDVKVSLFKK DKAMLFTYDQ YQENNVDQAS GSVLLHLEVG DQVWLQVYGE GERNGLYADN DNDSTFTGFL LYHDTN.
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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.
- View Data Sheet
Name :
Resistin Mutant HumanDescription:
Resistin Mutant Human Recombinant
Resistin, Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
Product # :
CYT-585Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
9.9 kDa protein containing 93 amino acid residues, produced in E.coli. Mutant-Resistin has had a Cysteine residue mutated to prevent dimerization and possibly acts as an antagonist.
Source
Escherichia Coli.
Formulation
Recombinant Human Resistin was lyophilized from a concentrated (1mg/ml) solution containing 0.1% TFA.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrophobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
Resistin may be an important link between obesity and insulin resistance. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity to insulin. Steppan et al. have suggested that resistin suppresses the ability of insulin to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity and is stimulated by several antidiabetic drugs.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression. -
Synonyms
Resistin, Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
-
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.
-
Solubility
Add 0.2 ml of deionized water and let the lyophilized pellet dissolve completely.
-
Amino Acid Sequence
MSSKTLCSME EAINERIQEV AGSLIFRAIS SIGLECQSVT SRGDLATCPR GFAVTGCTCG SACGSWDVRA ETTCHCQCAG MDWTGARCCR VQP.
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 :
PFN4 HumanDescription:
Profilin-4 Human Recombinant
PFN-4, Profilin-IV, Profilin4.
Product # :
PRO-818Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
PFN4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 149 amino acids (1-129 a.a.) and having a molecular mass of 16.4 kDa. PFN4 protein is fused to a 20 amino acid His tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
PFN4 Human solution containing 20mM Trsi HCL pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
PFN4 is a small actin-binding protein that participates in the dynamic turnover and restructuring of the actin cytoskeleton. PFN4 is localized in all eukaryotic organisms in the majority of cells. PFN4 is crucial for spatially and temporally controlled growth of actin microfilaments, which is a necessary process in cellular locomotion and cell shape changes.
-
Synonyms
PFN-4, Profilin-IV, Profilin4.
-
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 MSHLQSLLLD TLLGTKHVDS AALIKIQERS LCVASPGFNV TPSDVRTLVN GFAKNPLQAR REGLYFKGKD YRCVRADEYS LYAKNENTGV VVVKTHLYLL VATYTEGMYP SICVEATESL GDYLRKKGS.
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 :
PHB2 HumanDescription:
Prohibitin 2 Human Recombinant
BAP, Bap37, BCAP37, p22, PNAS-141, REA, Prohibitin-2, B-cell receptor-associated protein BAP37, D-prohibitin, Repressor of estrogen receptor activity, PHB2.
Product # :
PRO-1533Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
PHB2 Human Recombinant produced in E. coli is a single polypeptide chain containing 322 amino acids (1-299) and having a molecular mass of 35.7kDa. PHB2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PHB2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
Prohibitin 2, also known as PHB2, mediates transcriptional repression by nuclear hormone receptors via recruitment of histone deacetylases by similarity. PHB2 functions as an estrogen receptor (ER)-selective coregulator which potentiates the inhibitory activities of antiestrogens and represses the activity of estrogens. PHB2 which is involved in regulating mitochondrial respiration activity and in aging, competes with NCOA1 for modulation of ER transcriptional activity.
-
Synonyms
BAP, Bap37, BCAP37, p22, PNAS-141, REA, Prohibitin-2, B-cell receptor-associated protein BAP37, D-prohibitin, Repressor of estrogen receptor activity, PHB2.
-
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 MGSMAQNLKD LAGRLPAGPR GMGTALKLLL GAGAVAYGVR ESVFTVEGGH RAIFFNRIGG VQQDTILAEG LHFRIPWFQY PIIYDIRARP RKISSPTGSK DLQMVNISLR VLSRPNAQEL PSMYQRLGLD YEERVLPSIV NEVLKSVVAK FNASQLITQR AQVSLLIRRE LTERAKDFSL ILDDVAITEL SFSREYTAAV EAKQVAQQEA QRAQFLVEKA KQEQRQKIVQ AEGEAEAAKM LGEALSKNPG YIKLRKIRAA QNISKTIATS QNRIYLTADN LVLNLQDESF TRGSDSLIKG KK.
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 :
Eotaxin RatDescription:
Eotaxin Rat Recombinant (CCL11)
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11.
Product # :
CHM-260Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Eotaxin Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids and having a molecular mass of 8.4kDa. The CCL11 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in in 1×PBS, pH7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract purified blood eosinophils using a concentration range of 0.1-1.0 ug/ml, corresponding to a Specific Activity of 10-100IU/mg.More Info
-
Introduction
Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.
-
Synonyms
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Eotaxin although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution CCL11 should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Eotaxin in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
HPGSIPTSCC FTMTSKKIPN TLLKSYKRIT NNRCTLKAIV FKTKLGKEICADPKKKWVQD ATKHLDQKLQ TPKP.
-
Background
What is the molecular weight/Mw of EOTAXIN RAT Protein?
EOTAXIN RAT Protein has a total Mw of 8.4kDa.
What is the source or expression system of EOTAXIN RAT Protein?
Escherichia Coli.
What is the Purity of EOTAXIN RAT Protein?
EOTAXIN RAT Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of EOTAXIN RAT Protein?
Determined by its ability to chemoattract purified blood eosinophils using a concentration range of 0.1-1.0 ug/ml, corresponding to a Specific Activity of 10-100IU/mg.
What is the amino acid sequence of EOTAXIN RAT Protein?
HPGSIPTSCC FTMTSKKIPN TLLKSYKRIT NNRCTLKAIV FKTKLGKEICADPKKKWVQD ATKHLDQKLQ TPKP.
What applications can EOTAXIN RAT Protein be used in?
EOTAXIN RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EOTAXIN RAT Protein?
The endotoxin level is minimal, EOTAXIN RAT 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.
- View Data Sheet
Name :
ETNK2 HumanDescription:
EthanolamineKinase 2 Human Recombinant
Ethanolaminekinase-2
Product # :
PKA-077Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
ETNK2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 409 amino acids (1-386 a.a) and having a molecular mass of 47.2kDa.ETNK2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ETNK2 protein solution (0.25mg/ml) in Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
ETNK2 belongs to theethanolaminekinase family which catalyzes the 1st step of PtdEtn biosynthesis via the cytidine diphosphate.
-
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 MGSMAVPPSA PQPRASFHLR RHTPCPQCSW GMEEKAAASA SCREPPGPPR AAAVAYFGIS VDPDDILPGA LRLIQELRPH WKPEQVRTKR FTDGITNKLV ACYVEEDMQD CVLVRVYGER TELLVDRENE VRNFQLLRAH SCAPKLYCTF QNGLCYEYMQ GVALEPEHIR EPRLFRLIAL EMAKIHTIHA NGSLPKPILW HKMHNYFTLV KNEINPSLSA DVPKVEVLER ELAWLKEHLS QLESPVVFCH NDLLCKNIIY DSIKGHVRFI DYEYAGYNYQ AFDIGNHFNE FAGVNEVDYC LYPARETQLQ WLHYYLQAQK GMAVTPREVQ RLYVQVNKFA LASHFFWALW ALIQNQYSTI DFDFLRYAVI RFNQYFKVKP QASALEMPK.
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 :
PEDF PAT13D9AT AntibodyDescription:
Mouse Anti Human Pigment Epithelium-Derived Factor Clone PAT13D9AT
Pigment epithelium-derived factor,PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
Product # :
ANT-714Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
-
Introduction
PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. PEDF is a 50,000 dalton glycoprotein created and secreted in many tissues all the way through the body. A key component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. Additionally, PEDF is capable to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuro-protective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recognition of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities associate it as a potential therapeutic agent for the treatment of vasculature related neurodegenerative diseases such as age-related macular degeneration (AMD) and proliferative diabetic retinopathy (PDR). PEDF in addition has the potential to be functional in the treatment of various angiogenesis-related diseases including a number of cancers.
-
Synonyms
Pigment epithelium-derived factor,PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
-
Physical Appearance
Sterile filtered colorless solution.
-
Immunogen
Anti-human PEDF mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human PEDF protein 20-418 amino acids purified from E. coli.
-
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
-
Clone
PAT13D9AT.
-
Applications
PEDF antibody has been tested by ELISA, Western blot analysis and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
-
Type
Mouse Anti Human Monoclonal.
-
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
-
Purification Method
PEDF antibody was purified by protein-A affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
EGF Human, PichiaDescription:
Epidermal Growth Factor Human Recombinant, Pichia
Urogastrone, URG, EGF.
Product # :
CYT-332Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Epidermal Growth Factor Human Recombinant produced in Pichia Pastoris is a single, glycosylated, polypeptide chain containing 51 amino acids and having a molecular mass of 6KDa.The EGF is purified by proprietary chromatographic techniques.
Source
Pichia Pastoris.
Formulation
Lyophilized from a filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED₅₀, calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml corresponding to a specific activity of 1 x 107 Units/mg.
More Info
-
Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
-
Synonyms
Urogastrone, URG, EGF.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 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 Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.
-
Background
Harnessing Pichia for Epidermal Growth Factor Human Recombinant Production: Novel Approaches and Therapeutic Implications
Abstract:
This research paper delves into a cutting-edge avenue of Epidermal Growth Factor (EGF) Human Recombinant production by leveraging Pichia as an expression host. Through a synthesis of advanced methodologies encompassing genetic engineering, fermentation, and bioinformatics, this study explores the potential of Pichia-based platforms for enhanced EGF yield and biological activity. The findings not only offer insights into efficient EGF production but also underscore the therapeutic prospects of this approach.
Introduction:
Epidermal Growth Factor (EGF) holds a crucial place in cellular processes. This paper explores a novel dimension of EGF Human Recombinant production utilizing Pichia expression systems, emphasizing both technical aspects and the potential impact on therapeutic applications.
Pichia as an Expression Host:
Pichia stands as a promising alternative to conventional expression platforms due to its robustness and eukaryotic machinery. This paper investigates the strategic integration of EGF gene into Pichia, utilizing tailored vectors and promoters for optimal protein production.
Genetic Engineering Strategies:
Precise genetic manipulation is pivotal for enhanced EGF yield. Gene codon optimization and signal peptide selection are meticulously undertaken to ensure proper protein folding and secretion in Pichia. Through these approaches, EGF expression and secretion are finely tuned, resulting in biologically active EGF.
Fermentation and Protein Purification:
Expression is followed by fermentation in controlled conditions, leading to EGF accumulation. This step is supplemented by purification processes like chromatography, ensuring high EGF purity. Biochemical assays validate the biological activity of the purified EGF, affirming its therapeutic potential.
Bioinformatics in EGF-Pichia Interaction:
Advanced bioinformatics analyses shed light on the intricate interactions between EGF and Pichia host. Structural modeling and molecular dynamics simulations provide insights into potential post-translational modifications and protein-protein interactions, enriching our understanding of EGF behavior in Pichia.
Therapeutic Implications:
Beyond production, the paper emphasizes the therapeutic significance of EGF produced in Pichia. Enhanced production efficiency directly impacts cost-effectiveness, broadening its accessibility for therapeutic use. The EGF-Pichia approach presents exciting avenues for wound healing therapies and targeted cancer interventions.
Challenges and Future Directions:
Despite the progress, challenges such as glycosylation patterns and scaling-up strategies remain. Future efforts should focus on refining glycosylation profiles to ensure consistent bioactivity and optimizing bioreactor designs to scale up production for clinical applications.
Conclusion:
In a synergy of advanced methodologies and therapeutic implications, the Pichia-based Epidermal Growth Factor Human Recombinant production presents an innovative paradigm. The intricate harmony between Pichia host and EGF production holds promise for novel therapies, underscoring the potential impact of this pioneering approach.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6kDa.
What is the source or expression system of EGF Protein?
Pichia Pastoris.
What is the Purity of EGF Protein?
EGF Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EGF Protein?
The ED₅₀, calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml corresponding to a specific activity of 1 x 107 Units/mg.
What is the amino acid sequence of EGF Protein?
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.
What applications can EGF Protein be used in?
EGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, EGF 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.
- View Data Sheet
Name :
CDHR5 MouseDescription:
Cadherin Related Family Member 5 Mouse Recombinant
Cadherin-related family member 5, Mu-protocadherin, Cdhr5, Mucdhl, Mupcdh, 1810074H01Rik, AI481143
Product # :
PRO-2647Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CDHR5 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 621 amino acids (29-641 a.a) and having a molecular mass of 66.3kDa.CDHR5 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The CDHR5 solution (0.25mg/1ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
CDHR5, also referred to ascadherin-related family member 5, is a calcium-dependent cell adhesion protein. CDHR5 is located in coated pits, and is expressed during lung and kidney developmentat at the lateral and basal surfaces of epithelia.
-
Synonyms
Cadherin-related family member 5, Mu-protocadherin, Cdhr5, Mucdhl, Mupcdh, 1810074H01Rik, AI481143
-
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
QTQVCSVNQT IFRVEENTTV SEPLVNIFVP DGLHVTLGPL STPYAFRIEG KDLFLNVTPD YEENSLLQAD VECKRGDAVV VRLEVFVAVL DINDNAPKFS FEIKTFNVSE DTKVNTTVIP ETQLKATDAD INDILVYTLQ EVTPNASKFF SLEGVNYPAL KLDQTLDYFK NQNMTFMLLA RDTWEENVEP SHTATATLVL NTLPADLRTP WFLPCSFTDG YVCIHAQYSA VVPTGHKLPS PLIMSPGPIY AVDGDQAINQ SIIYSIIAGN TDGTFIINAH DGNLTMTKSI PSPMKFTLLI RADQEDMAQY SVTQAIVEAR SVTGNPLQFS QSLYYGTVVL GSEAGTAVKD KTFPSEILRI QAQYPGFPDL NSAVTYRVTN SSEFMMNKDI MLTAVPMEEA RTIRVEVEAS NTVTKDTATA VVEIQVSERE LPSTEFPTPP EAGGTTGPSS NTTMEAPLTS GTSQRPATTS SGGSVGPFPP GGTTLRPPTP ASSIPGGSPT LGTSTSPQTT TPGGDSAQTP KPGTSHPTAP TSRTSTSLMT TSSRSDSTQT PKPGTSQPMV PIPGASTSSQ PATPSGSSPQ TPKPGTSQST ATGPISGAGE QGDGQRFSTV DMALEHHHHH H
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
EDAR AntibodyDescription:
Ectodysplasin A Receptor, Mouse Anti Human
Ectodysplasin A Receptor, DL, Ectodysplasin 1, Anhidrotic Receptor, Anhidrotic Ectodysplasin Receptor 1, Ectodermal Dysplasia Receptor, Ectodysplasin-A Receptor, Downless Homolog, EDA-A1 Receptor, ECTD10A, ECTD10B, EDA3, HRM1, ED3, Tumor Necrosis Factor Receptor Superfamily Member EDAR, Downless, Mouse, Homolog Of, EDA-A1R, EDA1R, ED1R, ED5, Tumor necrosis factor receptor superfamily member EDAR.
Product # :
ANT-560Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
-
Introduction
Ectodysplasin A Receptor, also known as EDAR belongs to the tumor necrosis factor receptor family. EDAR is a receptor for the soluble ligand ectodysplasin A, and is capable of activating the nuclear factor-kappaB, JNK, as well as caspase-independent cell death pathways. EDAR is necessary for the development of hair, teeth, and other ectodermal derivatives. Furthermore, mutations in EDAR resulted in autosomal dominant and recessive forms of hypohidrotic ectodermal dysplasia.
-
Synonyms
Ectodysplasin A Receptor, DL, Ectodysplasin 1, Anhidrotic Receptor, Anhidrotic Ectodysplasin Receptor 1, Ectodermal Dysplasia Receptor, Ectodysplasin-A Receptor, Downless Homolog, EDA-A1 Receptor, ECTD10A, ECTD10B, EDA3, HRM1, ED3, Tumor Necrosis Factor Receptor Superfamily Member EDAR, Downless, Mouse, Homolog Of, EDA-A1R, EDA1R, ED1R, ED5, Tumor necrosis factor receptor superfamily member EDAR.
-
Physical Appearance
Sterile filtered colorless solution.
-
Immunogen
Anti-human EDAR mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human EDAR protein 27-448 amino acids purified from E. coli.
-
Ig Subclass
Mouse IgG2a heavy chain and k light chain.
-
Clone
PAT19E8AT.
-
Applications
EDAR antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.
-
Type
Mouse Anti Human Monoclonal.
-
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
-
Purification Method
EDAR antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TXN1 Human, HisDescription:
Thioredoxin Human Recombinant, His Tag
Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.
Product # :
PRO-804Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Thioredoxin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids (1-105 a.a.) and having a molecular mass of 13.9 kDa (Molecular weight on SDS-PAGE will appear higher). TXN protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
TXN1 solution containing 1x PBS pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is 7-10 A650/min/mg, obtained by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin.More Info
-
Introduction
Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation.
-
Synonyms
Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.
-
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 MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD DCQDVASECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT INELV.
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 :
Eptifibatide HumanDescription:
Eptifibatide Human
Product # :
PRO-358Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
Description
Synthetic Eptifibatide is a 6 amino acid peptide having a MW of 832.5 Dalton the following sequence Mpr-Har-Gly-Asp-Trp-Pro-Cys-NH2.
Formulation
Eptifibatide was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Eptifibatide binds to the platelet receptor glycoprotein (GP) IIb/IIIa of human platelets and inhibits platelet aggregation. Eptifibatide is a cyclic peptide derived from a protein discovered in the venom of the southeastern pygmy rattlesnake (Sistrurus miliarus barbouri). Eptifibatide belongs to the arginin-glycin-aspartat-mimetics and reversibly binds to platelets.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Eptifibatide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Eptifibatide 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 Eptifibatide in sterile 18MΩ-cm H2O 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.
- View Data Sheet
Name :
HTF HumanDescription:
Holo Transferrin Human
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.
Product # :
PRO-315Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Human Holo Transferrin is a glycoprotein of approximately 77 kDa.
Source
Human serum.
Formulation
The protein (10mg/ml) was lyophilized from 20mM NH4HC03 solution.
May contain traces of buffer salts.Purity
Greater than 98.0% as determined by coomassie blue stained SDS-PAGE and Cellulose Acetate electrophoresis.
More Info
-
Introduction
Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells. -
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.
-
Physical Appearance
Sterile Filtered Pink lyophilized (freeze-dried) powder.
-
Stability
Store the lyophilized Holo Transferrin between 2-8°C, do not freeze. Upon reconstitution Apo Transferrin 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 Holo Transferrin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Human Virus Test
FDA approved Plasma from each donor has been tested and found negative for antibodies to HIV-1 & 2, HCV, HBsAG, HBc, HBV, HAV, HIV and Syphilis.
-
Iron Content
The Iron content was estimated by ICP and was found to be 1232 ppm.
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 :
RARRES2 Human, HEKDescription:
Retinoic Acid Receptor Responder 2 Human Recombinant, HEK
Chemerin, TIG2, Tazarotene-induced gene 2 protein, Retinoic acid receptor responder protein 2, RAR-responsive protein TIG2, RARRES2, HP10433.
Product # :
PRO-2596Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
RARRES2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (21-157 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 143 amino acids and having a molecular mass of 16.6kDa. RARRES2 shows multiple bands between 13.5-18kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
HEK293.
Formulation
RARRES2 protein solution (0.5mg/ml) contains 10% glycerol & Phosphate buffered saline (pH7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
RARRES2 is a secreted chemotactic protein that initiates chemotaxis through the ChemR23 G protein-coupled seven-transmembrane domain ligand. RARRES2 is upregulated by the synthetic retinoid tazarotene and found in many tissues. RARRES2 acts as an adipokine and is truncated on both termini from the proprotein. RARRES2 is structurally related to the cathelicidin precursors, cystatin C and kininogens. RARRES2 promotes calcium mobilization and chemotaxis of immature dendritic cells and macrophages. RARRES2 is secreted as a precursor of little biological activity, which requires proteolytic cleavage of its COOH-terminal domain to be exchangeed into a potent and highly specific agonist of ChemR23.
-
Synonyms
Chemerin, TIG2, Tazarotene-induced gene 2 protein, Retinoic acid receptor responder protein 2, RAR-responsive protein TIG2, RARRES2, HP10433.
-
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
ELTEAQRRGL QVALEEFHKH PPVQWAFQET SVESAVDTPF PAGIFVRLEF KLQQTSCRKR DWKKPECKVR PNGRKRKCLA CIKLGSEDKV LGRLVHCPIE TQVLREAEEH QETQCLRVQR AGEDPHSFYF PGQFAFSHHH 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.
- View Data Sheet
Name :
VEGF (121 a.a.) HumanDescription:
Vascular Endothelial Growth Factor (121 a.a.) Human Recombinant
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Product # :
CYT-343Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Vascular Endothelial Growth Factor-121 Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide double chain containing 2x121 amino acids and having a molecular mass of 28.4kDa. VEGF121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
VEGF-121 has full biological activity when compared to standards. The activity is determined by the dose-dependent proliferation of HUVECs and is typically 1-6ng/ml corresponding to a specific activity of 166,667-1,000,000U/mg.
More Info
-
Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy. -
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Vascular Endothelial Growth Factor 121 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-121 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 Vascular Endothelial Growth Factor -121 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
APMAEGGGQN HHEVVKFMDV YQRSYCHPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TEESNITMQI MRIKPHQGQH IGEMSFLQHN KCECRPKKDR ARQENCDKPR 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.
- View Data Sheet
Name :
LHRH HumanDescription:
Luteinizing Hormone Releasing Hormone Human
Progonadoliberin-1, Progonadoliberin I, LHRH, GRH, GNRH, LNRH.
Product # :
HOR-261Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
Description
Lutenizing Hormone Releasing Hormone Human Synthetic is a single, non-glycosylated, polypeptide chain containing 10 amino acids and having a molecular mass of 1182.2 Dalton. The molecular formula is C55H75N17O13.C2H4O2. The CAS Number is 71447-49-9.
Formulation
The LHRH was lyophilized from a concentrated (1 mg/ml) solution with no additives.
Purity
Greater than 98.0% as determined by RP-HPLC.
More Info
-
Introduction
Gonadotropin-releasing hormone 1 (GNRH1), also known as Luteinising-hormone releasing hormone (LHRH), is a peptide hormone responsible for the release of FSH and LH from the anterior pituitary. GNRH1 is synthesized and released by the hypothalamus.
At the pituitary, GNRH1 stimulates the synthesis and secretion of the gonadotropins follicle-stimulating hormone (FSH) and luteinizing hormone (LH). These processes are controlled by the size and frequency of GNRH1 pulses, as well as by feedback from androgens and estrogens. Low requency GNRH1 pulses lead to FSH release, whereas high frequency GNRH1 pulses stimulate LH release.
There are differences in GNRH1 secretion between males and females. In males, GNRH1 is secreted in pulses at a constant frequency, but in females the frequency of the pulses varies during the menstrual cycle and there is a large surge of GNRH1 just before ovulation.
GNRH1 secretion is pulsatile in all vertebrates, and is necessary for correct reproductive function. Thus, a single hormone, GNRH1, controls a complex process of follicular growth, ovulation, and corpus luteum maintenance in the female, and spermatogenesis in the male. -
Synonyms
Progonadoliberin-1, Progonadoliberin I, LHRH, GRH, GNRH, LNRH.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized LHRH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LNRH 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 LHRH in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. The LHRH is also soluble in a 1% glacial acetic acid.
-
Amino Acid Sequence
Pyr-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2.
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 :
Cyclosporin ADescription:
Cyclosporin-A
Product # :
PRO-408Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Cyclosporin is a cyclic polypeptide immunosuppressant agent consisting of 11 amino acids and having a molecular weight of 1202.64. It is produced as a metabolite by the fungus species Beauveria nlyea. Chemically, cyclosporin is designated as [R-[R*,R*-(E)]]-cyclic(L-alanyl-D- alanyl-N-methyl-L-leucyl-N-methyl-L-leucyl-N-methyl-L-valyl-3-hydroxy-N, 4-dimethyl-L-2-amino-6-octenoyl-L-a-amino-butyryl- N-methylglycyl-N- methyl-L-leucyl-L-valyl-N-methyl-L-leucyl). Molecular Formula: C62H111N11O12.
Source
Beauveria Nivea.
Formulation
The Cyclosporin-A was lyophilized from a concentrated (1mg/ml) solution with no additives.
Purity
Greater than 99.0% as determined by RP-HPLC.
More Info
-
Introduction
Cyclosporin A is a noncytotoxic, natural, 11 amino acid cyclic peptide used clinically as an immunosuppressant for the treatment of autoimmune and inflammatory disorders and to prevent organ rejection after transplantation. Cyclosporin acts chiefly by inhibiting T lymphocyte function, which is vital for the propagation of inflammation. Cyclosporin A does not suppress the activity of other hematopoietic cells, does not cause bone marrow suppression and has a rapid onset of action as opposed to other immunosuppressive agents. Nevertheless, Cyclosporin A -induced nephrotoxicity remains an important clinical problem, and oxidative stress has been implicated as a potential responsible mechanism.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Cyclosporin A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Cyclosporin A 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 Cyclosporin-A in anhydrous ethanol R at a concentration of 50mg/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.
- View Data Sheet
Name :
MT IDescription:
Melanotan-I
Melanotan-I, MT-I, Melanotan-1.
Product # :
HOR-306Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
Description
Melanotan-I has the amino acid sequence of Ser-Tyr-Ser-Nle-Glu-His-D-Phe-Arg-Trp-Gly-Lys-Pro-Val and a molecular weight of 1647.4 Dalton.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 98.0% as determined by RP-HPLC.
More Info
-
Synonyms
Melanotan-I, MT-I, Melanotan-1.
-
Physical Appearance
Sterile Filtered off-White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Melanotan-I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MT-I 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 Melanotan-I in sterile 1% acetic acid not less than 100 µg/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.