Search results
1000 results found for “Ubiquitin”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
Adiponectin MouseDescription:
Adiponectin Mouse Recombinant
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-1168Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Acrp30 Mouse Recombinant is a single, glycosylated polypeptide chain containing 230 amino acids (18-247a.a) and having a molecular mass of 24.9kDa (calculated).
Source
HEK293 cells.
Formulation
Acrp30 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20mM Tris 50mM NaCl and 1mM CaCl2, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by its ability to inhibit proliferation of mouse 3T3 fibroblasts stimulated by PDGF. The ED50 for the effect is typically 5-15 μg/mL.
More Info
-
Introduction
Adiponectin, also known as Acrp30, AdipoQ and GBP-28, is a 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). Adiponectin is a part of 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; it does not show any change after two weeks at 4°C.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.
-
Amino Acid Sequence
EDDVTTTEEL APALVPPPKG TCAGWMAGIP GHPGHNGTPG RDGRDGTPGE KGEKGDAGLL GPKGETGDVG MTGAEGPRGF PGTPGRKGEP GEAAYVYRSA FSVGLETRVT VPNVPIRFTK IFYNQQNHYD GSTGKFYCNI PGLYYFSYHI TVYMKDVKVS LFKKDKAVLF TYDQYQEKNV DQASGSVLLH LEVGDQVWLQ VYGDGDHNGL YADNVNDSTF TGFLLYHDTN.
-
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 24.9kDa.
What is the source or expression system of ADIPONECTIN Protein?
HEK293 cells.
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 activity Measured by its ability to inhibit proliferation of mouse 3T3 fibroblasts stimulated by PDGF. The ED50 for the effect is typically 5-15 μg/mL.
What is the amino acid sequence of ADIPONECTIN Protein?
EDDVTTTEEL APALVPPPKG TCAGWMAGIP GHPGHNGTPG RDGRDGTPGE KGEKGDAGLL GPKGETGDVG MTGAEGPRGF PGTPGRKGEP GEAAYVYRSA FSVGLETRVT VPNVPIRFTK IFYNQQNHYD GSTGKFYCNI PGLYYFSYHI TVYMKDVKVS LFKKDKAVLF TYDQYQEKNV DQASGSVLLH LEVGDQVWLQ VYGDGDHNGL YADNVNDSTF TGFLLYHDTN.
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 :
BID HumanDescription:
BH3 Interacting Domain Death Agonist Human Recombinant
BH3-interacting domain death agonist, p22 BID, BID, FP497, MGC15319, MGC42355.
Product # :
PRO-627Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
BID Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids and having a molecular mass of 21.9 kDa.
Source
Escherichia Coli.
Formulation
The protein solution contains 20mM Tris-HCl pH-8 & 20% NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
BID accession number NP_001187 is a pro-apoptotic Bcl-2 protein having only the BH3 domain. In reaction to apoptotic signaling, BID interacts with another Bcl-2 family of cell death regulators, called Bax, they form a heterodimer resulting to the insertion of Bax into the outer mitochondrial membrane. Bax induces the opening of the mitochondrial voltage-dependent anion channel which lead to the release of cytochrome c and other pro-apoptotic factors from the mitochondria resulting in activation of caspases. BID is a mediator of mitochondrial damage induced by caspase-8 (CASP8). CASP8 cleaves BID, and the COOH-terminal part translocates to mitochondria where it triggers cytochrome c release. The major proteolytic product p15 BID releasea cytochrome c. Isoform 1, Isoform 2 and Isoform 4 induce ice-like proteases and apoptosis while Isoform 3 does not induce apoptosis.
-
Synonyms
BH3-interacting domain death agonist, p22 BID, BID, FP497, MGC15319, MGC42355.
-
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
MDCEVNNGSS LRDECITNLL VFGFLQSCSD NSFRRELDAL GHELPVLAPQ WEGYDELQTD GNRSSHSRLG RIEADSESQE
DIIRNIARHL AQVGDSMDRS IPPGLVNGLA LQLRNTSRSE EDRNRDLATA LEQLLQAYPR DMEKEKTMLV LALLLAKKVA SHTPSLLRDV FHTTVNFINQ NLRTYVRSLA RNGMD.
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 :
PAX8 HumanDescription:
Paired Box 8 Human Recombinant
Paired Box 8, Paired Box Gene 8, PAX8.
Product # :
PRO-2134Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
PAX8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 310 amino acids (1-287 a.a) and having a molecular mass of 33.4kDa.PAX8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PAX8 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Paired box 8, also known as PAX8 functions in thyroid follicular cell development as well as in expression of thyroid-specific genes. PAX8 complexes with TTF-1& TTF-2 in order to stimulate thyroid follicular cell differentiation and thyroid hormone biosynthesis by regulating the expression of NIS (sodium iodide symporter) , TPO (thyroid peroxidase), TG (thyroglobulin) and the TSHR (thyrotropin receptor). Defects in PAX8 are the cause of CHNG2 (congenital hypothyroidism non-goitrous type 2).
-
Synonyms
Paired Box 8, Paired Box Gene 8, PAX8.
-
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 MGSMPHNSIR SGHGGLNQLG GAFVNGRPLP EVVRQRIVDL AHQGVRPCDI SRQLRVSHGC VSKILGRYYE TGSIRPGVIG GSKPKVATPK VVEKIGDYKR QNPTMFAWEI RDRLLAEGVC DNDTVPSVSS INRIIRTKVQ QPFNLPMDSC VATKSLSPGH TLIPSSAVTP PESPQSDSLG STYSINGLLG IAQPGSDKRK MDDSDQDSCR LSIDSQSSSS GPRKHLRTDA FSQHHLEPLE CPFERQHYPE AYASPSHTKG EQEVNTLAMP MATPPTPPTA RPGASPTPAC
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 :
Leptin qA Mouse, PEGDescription:
Leptin Quadruple Antagonist Pegylated Mouse Recombinant
Product # :
CYT-1244Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Leptin Antagonist Quadruple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Mouse Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. The Mouse Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Mouse Leptin Quadruple anatagonist Pegylated runs as a 55 kDa due to enlarged hydrodymanic volume. Leptin Antagonist Quadruple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Mouse Leptin Quadruple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Pegylated Mouse Leptin Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated recombinant mouse leptin antagonist in vitro activity is 6-8 fold lower than the non-pegylated recombinant super mouse leptin antagonist but in vivo it has profound weight gain effect, resulting mainly from increased food intake. Its in vivo activity compared to that of PEG-MLA is 9-27 fold higher.
More Info
-
Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Leptin Antagonist Quadruple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
-
Background
Leptin produced mainly by adipocytes. Leptin mostly regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
-
Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SERPINA1 Human, ActiveDescription:
Alpha-1 Antitrypsin, Active Human Recombinant
Alpha-1-antitrypsin, Alpha-1 protease inhibitor, Alpha-1-antiproteinase, SERPINA1, A1AT, PI, A1A, AAT, PI1, MGC9222, PRO2275, MGC23330.
Product # :
PRO-907Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
SERPINA1 Human Recombinant produced in rice is a single, non-glycosylated polypeptide chain containing 384 amino acids and having a molecular mass of 43.1 kDa.The SERPINA1 protein is purified by proprietary chromatographic techniques.
Source
Rice Grain (Oryza Sativa).
Formulation
SERPINA1 was lyophilized from a concentrated solution containing recombinant Albumin.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
3~5 mg SERPINA1 will inhibit 1 mg PPE with an activity of 10.8 units per mg proteinMore Info
-
Introduction
SERPINA1 is secreted and is a serine protease inhibitor which its targets include elastase, plasmin, collagenase, leucocytic proteases, trypsin, chymotrypsin, and plasminogen activator. Defects in SERPINA1 gene can cause emphysema or liver disease. SERPINA1 is an endogenous inhibitor of serine proteases and inhibits the catalytic domain of human recombinant matriptase in vitro. Rise in SERPINA1 occurs as an acute phase response to tissue necrosis and inflammation. mutations in SERPINA1 and SLC11A1 genes change the balance between elastase produced by leukocytes during phagocytosis.
-
Synonyms
Alpha-1-antitrypsin, Alpha-1 protease inhibitor, Alpha-1-antiproteinase, SERPINA1, A1AT, PI, A1A, AAT, PI1, MGC9222, PRO2275, MGC23330.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized SERPINA1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SERPINA1 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 SERPINA1 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 :
IL 33 RatDescription:
Interleukin-33 Rat Recombinant
Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, NFEHEV, DKFZp586H0523, RP11-575C20.2, IL-33.
Product # :
CYT-150Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
IL 33 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 156 amino acids and having a molecular mass of 17.4kDa.The IL 33 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was determined by the dose-dependent stimulation of the proliferation of murine D10S cells is <0.5ng/ml, corresponding to a specific activity of >2,000,000units/mg.More Info
-
Introduction
Interleukin 33 (IL-33) is a 32kDa proinflammatory cytokine that may also regulate gene transcription in producer cells. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1 (IL1 receptor-like-1), which is known also as ST2. Binding of IL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces expression of IL-4, IL-5, IL-13 and leads to severe pathological changes in mucosal organs and in vitro, it can be divided to N-terminal fragment of 12kDa and C-terminal fragment of 18kDa by cleavage of caspase-1.
-
Synonyms
Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, NFEHEV, DKFZp586H0523, RP11-575C20.2, IL-33.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized IL-33 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-33 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 IL-33 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
SIQGTSLLTE SCALSTYNDQ SVSFVLENGC YVINVEDCGK NQEKDKVLLR YYESSFPAQS GDGVDGKKLM VNMSPIKDTD IWLNANDKDY SVELQKGDVS PPDQAFFVLH KKSSDFVSFE CKNLPGTYIG VKDNQLALVE ENDESCNNIM FKLSKM
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 :
SARS Envelope, HisDescription:
SARS-Associated Coronavirus Envelope Recombinant, His Tag
Product # :
SARS-004Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
The E.coli derived recombinant protein contains the Envelope protein 1-76 amino acids immunodominant regions fused to 6xHis tag at C-terminal.
Source
Escherichia Coli.
Formulation
SARS Envelope protein solution is supplied in PBS.
Purity
Protein is >90% pure as determined SDS-PAGE.
More Info
-
Introduction
SARS Associated Coronavirus Envelope is a small membrane protein that takes major part in the life cycle of the virus. This protein is needed for the assembly, budding, creation of the envelope and pathogenesis. This protein contains 3 outer structural proteins, the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to assure viral entry thetarget cells. Accordingly, S-protein has a major part in virus infection cycle and is the mainly target of neutralizing antibodies.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Protein is shipped on ice packs. Upon arrival, Store at -20°C.
-
Specificity
Immunoreactive with sera of SARS-infected individuals.
-
Purification Method
Purified by proprietary chromatographic technique.
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 :
Aprotinin ProteinDescription:
Aprotinin
Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.
Product # :
PRO-285Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- More Info
Description
Aprotinin is a natural proteinase inhibitor polypeptide consisting of fifty-eight amino acids {C284H432N84O79S7} arranged in a single polypeptide chain, cross-linked by three disulfide bridges and having a molecular mass of 6512.
Source
Bovine Lung.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
More Info
-
Introduction
Aprotinin inhibits the activity of several proteolytic enzymes such as chymotrypsin, kallikrein, plasmin and trypsin. Aprotinin is present in blood and in most tissues, with a high concentration in lung. Aprotinin inhibits pro-inflammatory cytokine release and maintains glycoprotein homeostasis. In platelets, aprotinin reduces glycoprotein loss (e.g., GpIb, GpIIb/IIIa), while in granulocytes it prevents the expression of pro-inflammatory adhesive glycoproteins (e.g., CD11b).
-
Synonyms
Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Aprotinin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Aprotinin 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 Aprotinin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Specific Activity
5,940 KIU (Kallikrein Inactivator Units) per mg, 3.3 pH.Eur.U/mg.
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 :
C.Albicans EnolaseDescription:
Candida Albicans Enolase Recombinant
Product # :
PRO-2297Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Candida Albicans Enolase produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 46kDa. C.Albicans Enolase is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
C.Albicans Enolase is supplied in 20mM HEPES buffer pH-8, 200mM NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Candida albicans is a diploid fungus, which grows both as yeast and filamentous cells and a contributory agent of opportunistic oral and genital infections in humans, and candidal onychomycosis (an infection of the nail plate). Systemic fungal infections (fungemias) including those by C. albicans are regarded as key causes of morbidity and mortality in immunocompromised patients (e.g., AIDS, cancer chemotherapy, organ or bone marrow transplantation). C. albicans biofilms may develop on the surface of implantable medical devices. C. albicans is commensal and a constituent of the normal gut flora containing microorganisms which live in the human mouth and gastrointestinal tract. Overgrowth of the fungus leads to in candidiasis (candidosis). Candidiasis is frequently detected in immunocompromised persons, including HIV-infected patients. To infect host tissue, the habitual unicellular yeast-like form of C. albicans reacts to environmental signals and changes into an invasive, multicellular filamentous form, a phenomenon which is known as dimorphism.
-
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. 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.
- View Data Sheet
Name :
GAGA-POZDescription:
GAGA-POZ Drosophila Melanogaster Recombinant
Transcription factor GAGA, Trithorax-like protein, GAGA factor, GAF, Adh transcription factor 2, Neural conserved at 70F, Trl, Adf-2, GAGA, Nc70F, TFGAGA, CG33261, GAGA-POZ.
Product # :
PRO-435Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GAGA-POZ Drosophila Melanogaster Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids & having a molecular mass of 14 kDa.
Source
Escherichia Coli.
Formulation
The protein containing 10mM HEPES (pH-7.4) and 25mM NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
The GAGA factor is a sequence-specific DNA-binding protein, which participates in the regulation of the expression of a variety of different classes of genes in Drosophila such as many developmentally regulated genes, stress induced genes, and cell cycle regulated genes, as well as housekeeping genes. GAGA contains a C-terminal glutamine-rich domain and a highly conserved N-terminal POZ domain which reported to be involved in self-oligomerization in a number of other POZ domain containing proteins. In case of GAGA protein, the N-terminal POZ domain mediates the formation of oligomers both in vitro and in vivo.
-
Synonyms
Transcription factor GAGA, Trithorax-like protein, GAGA factor, GAF, Adh transcription factor 2, Neural conserved at 70F, Trl, Adf-2, GAGA, Nc70F, TFGAGA, CG33261, GAGA-POZ.
-
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
MSLPMNSLYS LTWGDYGTSL VSAIQLLRCH GDLVDCTLAA GGRSFPAHKI VLCAASPFLLDLLKNTPCKH PVVMLAGVNA NDLEALLEFV YRGEVSVDHA QLPSLLQAAQ CLNIQGLAPQTVTKDDYTTH.
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 :
WWTR1 HumanDescription:
WW Domain Containing Transcription Regulator 1 Human Recombinant
WW domain-containing transcription regulator protein 1, Transcriptional coactivator with PDZ-binding motif, WWTR1, WW Domain Containing Transcription Regulator 1, TAZ.
Product # :
PRO-1814Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
WWTR1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 423 amino acids (1-400) and having a molecular mass of 46.5 kDa.WWTR1 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The WWTR1 solution (0.5mg/ml) contains 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
-
Introduction
WW Domain Containing Transcription Regulator 1 (WWTR1) is a transcriptional coactivator that plays a role as a downstream regulatory target in the Hippo signaling pathway which participates in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. WWTR1 regulates the nuclear accumulation of SMADS and has a main part in coupling them to the transcriptional machinery like the mediator complex. WWTR1 is also regulates embryonic stem-cell self-renewal.
-
Synonyms
WW domain-containing transcription regulator protein 1, Transcriptional coactivator with PDZ-binding motif, WWTR1, WW Domain Containing Transcription Regulator 1, TAZ.
-
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 MGSMNPASAP PPLPPPGQQV IHVTQDLDTD LEALFNSVMN PKPSSWRKKI LPESFFKEPD SGSHSRQSST DSSGGHPGPR LAGGAQHVRS HSSPASLQLG TGAGAAGSPA QQHAHLRQQS YDVTDELPLP PGWEMTFTAT GQRYFLNHIE KITTWQDPRK AMNQPLNHMN LHPAVSSTPV PQRSMAVSQP NLVMNHQHQQ QMAPSTLSQQ NHPTQNPPAG LMSMPNALTT QQQQQQKLRL QRIQMERERI RMRQEELMRQ EAALCRQLPM EAETLAPVQA AVNPPTMTPD MRSITNNSSD PFLNGGPYHS REQSTDSGLG LGCYSVPTTP EDFLSNVDEM DTGENAGQTP MNINPQQTRF PDFLDCLPGT NVDLGTLESE DLIPLFNDVE SALNKSEPFL TWL.
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 :
C8 HumanDescription:
Complement C8 Human
Product # :
PRO-2695Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Human Complement C8 produced in Human plasma is glycosylated polypeptide chain conteining 3 chains and having a total molecular mass of 151kDa.
Source
Human Plasma.
Formulation
C8 protein solution contains PBS pH 7.2.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Native human C8 is a glycosylated protein consist of 3 polypeptide chains: The alpha chain and the gamma chain are disulfide linkedwhereas, The beta chain is non-covalently bound to the a-g complex. C8 is necessary for formation of the membrane attack complex and is activated by binding on the cell membrane newly-formed C5b,C6,C7 complexes. Each pathway of complement activation generates proteolytic enzyme complexes which bind the target surface. These enzymes cleave a peptide bond in the larger alpha chain of C5 releasing C5a and activating C5b. Although C5b is unstable it remains bound to the activating complex for a few minutes during which it binds a single C6 from the surrounding fluid or it decays and is no longer capable of forming MAC.The C5b,6 complex may also remain connected to the C3/C5 convertase where the binding of a single C7 exposes a membrane-binding region and C5b,6,7 can enter into the bilipid layer of the target cell. Each C5b-7 complex can bind 1 molecule of C8 causing the complex to enter more firmly into the membrane.
-
Physical Appearance
Sterile filtered solution.
-
Stability
C8 Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.
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 :
Globular Adiponectin MouseDescription:
Globular Adiponectin Mouse Recombinant
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-432Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- sds-page
Description
The globular domain of Adiponectin Mouse Recombinant / Acrp30 Mouse contains 138 amino acid residues from a.a. 111-247 having molecular mass of 16 kDa was over expressed in E.coli and purified by using conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
Acrp30 Mouse (1mg/ml) solution containing 20mM Tris-HCl pH7.5, 50mM NaCl, 5mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
More Info
-
Introduction
Adiponectin (247amino acids) is adipocyte complement-related protein of 30 kDa and exclusively expressed in differentiated adipocytes. APM-1 (Acrp30 Mouse) is a member of the complement factor C1q family and consists of signal sequence, Non-homologous sequence, collagen domain and domain (gAcrp30).
Adiponectin expression is reduced in a variety of obese and insulin-resistant states in human, monkeys and mice. Injection of Acrp30 Mouse (247aa) or gAcrp30 (globular domain) lowers serum glucose and free fatty acid level in mice. -
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
-
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
MAYMYRSAFS VGLETRVTVP NVPIRFTKIF YNQQNHYDGS TGKFYCNIPG LYYFSYHITVYMKDVKVSLF KKDKAVLFTY DQYQEKNVDQ ASGSVLLHLE VGDQVWLQVY GDGDHNGLYADNVNDSTFTG FLLYHDTN
-
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 16kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% 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?
MAYMYRSAFS VGLETRVTVP NVPIRFTKIF YNQQNHYDGS TGKFYCNIPG LYYFSYHITVYMKDVKVSLF KKDKAVLFTY DQYQEKNVDQ ASGSVLLHLE VGDQVWLQVY GDGDHNGLYADNVNDSTFTG FLLYHDTN
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 :
FKBP4 HumanDescription:
FK506 Binding Protein 4 Human Recombinant
HBI, p52, Hsp56, FKBP52, FKBP59, PPIase, FKBP4, FK506-binding protein 4, Peptidyl-prolyl cis-trans isomerase, HSP-binding immunophilin, FKBP52 protein, 52 kDa FK506-binding protein, p59 protein.
Product # :
ENZ-412Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
FKBP4 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 479 amino acids (1-459 a.a.) and having a molecular mass of 53.9 kDa.FKBP4 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FKBP4 protein solution contains 20mM Tris-HCl, pH-8 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 300 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH 8.0 using chymotrypsin.More Info
-
Introduction
FKBP4 is part of the immunophilin protein family, which takes part in immunoregulation and necessary cellular processes concerning protein folding and trafficking. FKBP4 is a cis-trans prolyl isomerase that connects to the immunosuppressants FK506 and rapamycin. FKBP4 has high structural and functional similarity to FKBP1A, though, FKBP4 does not have immunosuppressant activity when complexed with FK506. FKBP4 is known to connect with phytanoyl-CoA alpha-hydroxylase. FKBP4 associates with HSP90 & HSP70 thus takes part in the intracellular trafficking of hetero-oligomeric forms of the steroid hormone receptors. FKBP4 highly associates with adeno-associated virus type 2 vectors (AAV) resulting in a considerable increase in AAV-mediated transgene expression in human cell lines. FKBP4 is involved in the optimal use of AAV vectors in human gene therapy.
-
Synonyms
HBI, p52, Hsp56, FKBP52, FKBP59, PPIase, FKBP4, FK506-binding protein 4, Peptidyl-prolyl cis-trans isomerase, HSP-binding immunophilin, FKBP52 protein, 52 kDa FK506-binding protein, p59 protein.
-
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 MTAEEMKATE SGAQSAPLPM EGVDISPKQD EGVLKVIKRE GTGTEMPMIG DRVFVHYTGW LLDGTKFDSS LDRKDKFSFDLGKGEVIKAW DIAIATMKVG EVCHITCKPE YAYGSAGSPP KIPPNATLVF EVELFEFKGE DLTEEEDGGI IRRIQTRGEG YAKPNEGAIV EVALEGYYKDKLFDQRELRF EIGEGENLDL PYGLERAIQR MEKGEHSIVY LKPSYAFGSV GKEKFQIPPN AELKYELHLK SFEKAKESWE MNSEEKLEQS TIVKERGTVYFKEGKYKQAL LQYKKIVSWL EYESSFSNEE AQKAQALRLA SHLNLAMCHL KLQAFSAAIE SCNKALELDS NNEKGLFRRG EAHLAVNDFE LARADFQKVLQLYPNNKAAK TQLAVCQQRI RRQLAREKKL YANMFERLAE EENKAKAEAS SGDHPTDTEM KEEQKSNTAG SQSQVETEA.
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 :
Streptolysin-ODescription:
Streptolysin-O Streptococcus Pyogenes Recombinant
Streptolysin O, Thiol-activated cytolysin, slo.
Product # :
PRO-2302Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Streptococcus Pyogenes Streptolysin-O produced in E.coli is a single, non-glycosylated, polypeptide chain containing 538 amino acids and having a molecular mass of 60.1kDa.The Streptolysin-O is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Streptolysin-O protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Streptolysin-O is a sulfhydryl-activated toxin which causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the Streptolysin-O protein undergoes a major conformation change, leading to its insertion in the host membrane and creation of an oligomeric pore complex. Cholesterol may be needed for binding to host membranes, membrane insertion and pore formation. Streptolysin-O can be reversibly inactivated by oxidation.
-
Synonyms
Streptolysin O, Thiol-activated cytolysin, slo.
-
Physical Appearance
Sterile Filtered white lyophilized powder.
-
Stability
Lyophilized Streptolysin-O although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Streptolysin-O 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 Streptolysin-O in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
NKQNTASTET TTTNEQPKPE SSELTTEKAG QKTDDMLNSN DMIKLAPKEM PLESAEKEEK KSEDKKKSEE DHTEEINDKI YSLNYNELEV LAKNGETIEN FVPKEGVKKA DKFIVIERKK KNINTTPVDI SIIDSVTDRT YPAALQLANK GFTENKPDAV VTKRNPQKIH IDLPGMGDKA TVEVNDPTYA NVSTAIDNLV NQWHDNYSGG NTLPARTQYT ESMVYSKSQI EAALNVNSKI LDGTLGIDFK SISKGEKKVM IAAYKQIFYT VSANLPNNPA DVFDKSVTFK ELQRKGVSNE APPLFVSNVA YGRTVFVKLE TSSKSNDVEA AFSAALKGTD VKTNGKYSDI LENSSFTAVV LGGDAAEHNK VVTKDFDVIR NVIKDNATFS RKNPAYPISY TSVFLKNNKI AGVNNRTEYV ETTSTEYTSG KINLSHQGAY VAQYEILWDE INYDDKGKEV ITKRRWDNNW YSKTSPFSTV IPLGANSRNI RIMARECTGL AWEWWRKVID ERDVKLSKEI NVNISGSTLS PYGSITYK.
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 Mouse, BiotinDescription:
Epidermal Growth Factor Mouse Recombinant, Biotin
Urogastrone, URG, EGF.
Product # :
CYT-841Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
EGF Mouse Recombinant, Biotin produced in E.Coli is a non-glycosylated polypeptide chain containing 61 amino acids and having a total molecular mass of 7.0kDa. This version of EGF has a N terminal leader sequence hosting a biotin conjugation. There are 0.5 biotins for each EGF protein.
Source
Escherichia Coli.
Formulation
The protein (0.5mg/ml) solution contains sterile PBS.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells is 0.14-0.2ng/ml, corresponding to a specific activity of 7.1x106units/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 clear solution.
-
Stability
Should be stored at 4°C.Please do not freeze.
-
Amino Acid Sequence
MKKIDDDKNS YPGCPSSYDG YCLNGGVCMH IESLDSYTCN CVIGYSGDRC QTRDLEWWEL R.
-
Background
Synergistic Explorations: Epidermal Growth Factor Mouse Recombinant and Biotin Conjugation for Enhanced Therapeutic Potential
Abstract:
This research paper delves into the innovative convergence of Epidermal Growth Factor Mouse Recombinant (EGF-MR) and biotin conjugation, unraveling their intricate interplay, molecular attributes, and therapeutic implications. By employing cutting-edge methodologies involving protein engineering, conjugation chemistry, and cellular assays, this study uncovers the augmented cellular responses driven by EGF-MR-biotin complex. The findings highlight a novel avenue for tailored regenerative medicine and targeted therapy.
Introduction:
Epidermal Growth Factor (EGF) governs pivotal cellular processes. This paper navigates the unexplored realm of Epidermal Growth Factor Mouse Recombinant (EGF-MR) in synergy with biotin conjugation, elucidating their combined molecular attributes and therapeutic potential.
Protein Engineering and Biotin Conjugation:
EGF-MR is strategically engineered to enable biotin conjugation, a process that enhances targeting and delivery. This paper delves into site-specific modification approaches, ensuring precise and controlled conjugation of biotin moieties to EGF-MR.
Cellular Signaling Amplification:
The EGF receptor (EGFR) activation triggers cascades of intracellular events. Structural studies and binding kinetics illuminate how the biotin-conjugated EGF-MR modulates EGFR interactions, amplifying downstream signaling pathways like the MAPK and PI3K/Akt cascades.
Cellular Assays and Functional Responses:
In vitro cellular assays, encompassing cell proliferation and migration studies, elucidate the effect of EGF-MR-biotin complex on cellular responses. Live-cell imaging techniques reveal enhanced cell motility and survival, underpinning the potential therapeutic impact.
Tailored Delivery Strategies:
The biotin-avidin interaction offers a strategic avenue for targeted drug delivery. Employing this interaction, EGF-MR-biotin complex can be directed to specific cell types, revolutionizing precision medicine and enabling tailored therapeutic interventions.
Regenerative Medicine and Targeted Therapy:
The augmented cellular responses initiated by EGF-MR-biotin complex hold significant promise. In regenerative medicine, the complex's potential to accelerate tissue regeneration becomes evident. Furthermore, in targeted therapy, the complex's enhanced cellular uptake offers a novel approach to modulate tumor microenvironments.
Future Prospects and Challenges:
While transformative, challenges persist, including optimizing conjugation efficiency and unraveling long-term effects. Future research should focus on refining delivery strategies and conducting comprehensive long-term studies to harness the full therapeutic potential.
Conclusion:
In a convergence of ingenious methodologies and visionary therapeutic approaches, the synergy between Epidermal Growth Factor Mouse Recombinant and biotin emerges as a captivating frontier. The molecular marriage between EGF-MR and biotin not only amplifies cellular responses but also opens doors for targeted interventions and precision therapies, revolutionizing the landscape of medical advancements.
What is the molecular weight/Mw of MEGF, BIOTIN Protein?
MEGF, BIOTIN Protein has a total Mw of 7kDa.
What is the source or expression system of MEGF, BIOTIN Protein?
Escherichia Coli.
What is the Purity of MEGF, BIOTIN Protein?
MEGF, BIOTIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of MEGF, BIOTIN Protein?
The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells is 0.14-0.2ng/ml, corresponding to a specific activity of 7.1x106units/mg.
What is the amino acid sequence of MEGF, BIOTIN Protein?
MKKIDDDKNS YPGCPSSYDG YCLNGGVCMH IESLDSYTCN CVIGYSGDRC QTRDLEWWEL R.
What applications can MEGF, BIOTIN Protein be used in?
MEGF, BIOTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for MEGF, BIOTIN Protein?
The endotoxin level is minimal, MEGF, BIOTIN 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 :
IGF1 E3R HumanDescription:
Insulin Like Growth Factor-1, Mutant E3R Human Recombinant
Insulin-Like Growth Factor-1.
Product # :
CYT-1217Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
IGF1 E3R Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids (Gly49-Ala118) and having a molecular mass of 8.6kDa. IGF1 E3R Human is fused to a 6 a.a his tag at C-Terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The filtered (0.4µm) concentrated protein solution was lyophilized from 0.5mg/ml solution in 50 mM NaCl, 20 mM Tris and 5% (w/v) trehalose, pH 8.0.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Synonyms
Insulin-Like Growth Factor-1.
-
Physical Appearance
Sterile 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 prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. IGF1 E3R is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
MGPRTLCGAE LVDALQFVCG DRGFYFNKPT GYGSSSRRAP QTGIVDECCF RSCDLRRLEM YCAPLKPAKS AHHHHHH.
-
Background
Insulin-like Growth Factor 1 (IGF-1) is a critical peptide hormone that plays a central role in regulating growth and development. Genetic mutations in the IGF-1 gene can result in altered IGF-1 variants, leading to various physiological consequences. Understanding these IGF-1 mutants is of paramount importance as they offer insights into growth disorders, metabolic regulation, and potential therapeutic avenues. This research delves into the world of IGF-1 mutants, shedding light on their diverse functions and implications for human health.
The primary objective of this research is to elucidate the impact of IGF-1 mutations on growth regulation. In vitro and in vivo experiments will be conducted to investigate how these mutants interact with IGF-1 receptors, influence downstream signaling pathways, and modulate growth plate dynamics. Understanding these mechanisms is crucial for unraveling the complexities of growth disorders associated with IGF-1 mutations.
The second objective is to assess the clinical relevance of IGF-1 mutants in growth-related conditions. Clinical studies involving individuals with growth hormone deficiencies or growth disorders linked to IGF-1 mutations will be conducted to evaluate the effects of these mutants on stature and overall health. These investigations may provide valuable insights into potential therapeutic strategies for individuals affected by growth-related disorders.
The third objective is to explore the broader implications of IGF-1 mutants in metabolic regulation and age-related conditions. Research will investigate their roles in metabolic homeostasis, longevity, and susceptibility to age-related diseases. Understanding the multifaceted properties of IGF-1 mutants may open new avenues for therapeutic interventions in various health and aging-related conditions.
By delving into the diverse functions of IGF-1 mutants, this research aims to expand our understanding of their physiological roles and clinical applications. The findings may contribute to the development of targeted interventions for growth disorders, metabolic conditions, and age-related diseases.
What is the molecular weight/Mw of IGF1 E3R HUMAN Protein?
IGF1 E3R HUMAN Protein has a total Mw of 8.6kDa.
What is the source or expression system of IGF1 E3R HUMAN Protein?
Escherichia Coli.
What is the Purity of IGF1 E3R HUMAN Protein?
IGF1 E3R HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IGF1 E3R HUMAN Protein?
The biological functionality of IGF1 E3R HUMAN Protein will be determined in the future.
What is the amino acid sequence of IGF1 E3R HUMAN Protein?
MGPRTLCGAE LVDALQFVCG DRGFYFNKPT GYGSSSRRAP QTGIVDECCF RSCDLRRLEM YCAPLKPAKS AHHHHHH.
What applications can IGF1 E3R HUMAN Protein be used in?
IGF1 E3R HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IGF1 E3R HUMAN Protein?
The endotoxin level is minimal, IGF1 E3R 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 :
Omentin Human, HisDescription:
Omentin Human Recombinant, His Tag
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
Product # :
CYT-551Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Omentin Human Recombinant is produced in E.Coli by recombinant DNA technology is a single, polypeptide chain containing 294 amino acids and having a molecular mass of 32.7 kDa. Recombinant Human Omentin contains His tag fused at N-Terminus.Intelectin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Each mg of lyophilized powder contains 20mM Tris & 50mM NaCl pH-8.0.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase insulin-stimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of insulin presence. Its role in glucose metabolism and obesity remains to be described; an insulin-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.
-
Synonyms
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Intelectin His Tag although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Intelectin 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 Omentin His Tag in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MRGSHHHHHH GMASTDEANT YFKEWTCSSS PSLPRSCKEI KDECPSAFDG LYFLRTENGV IYQTFCDMTS GGGGWTLVAS VHENDMRGKC TVGDRWSSQQ GSKAVYPEGD GNWANYNTFG SAEAATSDDY KNPGYYDIQA KDLGIWHVPN KSPMQHWRNS SLLRYRTDTG FLQTLGHNLF GIYQKYPVKY GEGKCWTDNG PVIPVVYDFG DAQKTASYYS PYGQREFTAG FVQFRVFNNE RAANALCAGM RVTGCNTEHH CIGGGGYFPE ASPQQCGDFS GFDWSGYGTH VGYS.
-
Applications
Elisa
Western blot.
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 :
TROVE2 Human, His BiotinDescription:
TROVE Domain Family Member 2 Human Recombinant, His Tag Biotinylated
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
Product # :
PRO-2560Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TROVE2 Human Recombinant Biotin produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 56kDa. The TROVE2 is expressed with a 6xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein solution contains 20mM HEPES (pH 8.0), 20% Glycerol and 150mM NaCl.
Purity
Greater than 89% as determined by Capillary Electrophoresis.
More Info
-
Introduction
Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.
-
Synonyms
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
-
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. 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.
- View Data Sheet
Name :
OPG HumanDescription:
Osteoprotegerin Human Recombinant
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, Osteoprotegerin, TR1, MGC29565.
Product # :
CYT-177Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Recombinant Human Osteoprotegerin produced in E.coli cells is a single, non-glycosylated, polypeptide chain containing 174 amino acids and having a molecular mass of 20kDa. The OPG is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OPG was lyophilized from a 0.2µm filtered concentrated (0.5mg/ml) solution in PBS, pH 7.4.
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 its ability to neutralize the stimulation of U937 cells treated with 10ng/ml of soluble RANKL corresponding to a specific activity of 100,000IU/mg.More Info
-
Introduction
Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.
-
Synonyms
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, Osteoprotegerin, TR1, MGC29565.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Osteoprotegerin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution OCIF 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 Osteoprotegerin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
METFPPKYLH YDEETSHQLL CDKCPPGTYL KQHCTAKWKT VCAPCPDHYY TDSWHTSDEC LYCSPVCKEL QYVKQECNRT HNRVCECKEG RYLEIEFCLK HRSCPPGFGV VQAGTPERNT VCKRCPDGFF SNETSSKAPC RKHTNCSVFG LLLTQKGNAT HDNICSGNSE STQK.
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 :
LGALS3 HumanDescription:
Galectin-3 Human Recombinant
Galectin-3, GAL3, MAC2, CBP35, GALB, GALIG, LGALS2, LGALS3, Galactose-specific lectin 3, Mac-2 antigen, IgE-binding protein, 35 kDa lectin, Carbohydrate-binding protein 35, CBP 35, Laminin-binding protein, Lectin L-29, L-31, Galactoside-binding protein, GALBP.
Product # :
CYT-606Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
LGALS3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 250 amino acids and having a molecular mass of 26.2kDa. The LGALS3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Galectin-3 protein was lyophilized from a sterile 0.2 micron filtered aqueous solution containing 10 mM sodium phosphate and 50mM sodium chloride, pH 7.5.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
More Info
-
Introduction
Galectin-3 mediates with the alpha-3, beta-1 integrin the stimulation by cspg4 of endothelial cells migration. Galectin-3 plays an necessary part during the acquisition of vasculogenic mimicry and angiogenic properties associated with melanoma progression. LGALS3 overexpression is highly expressed in early stages of papillary carcinoma, and its expression intensity declines during tumor progression. Serum levels of LGALS3 are high in patients with thyroid malignancy but there is considerable overlap in serum LGALS3 concentrations between those with benign and malignant nodular thyroid disease. LGLAS3 takes part as an immune regulator to inhibit T-cell immune responses and promote tumor growth, as a result providing a new mechanism for tumor immune tolerance.
-
Synonyms
Galectin-3, GAL3, MAC2, CBP35, GALB, GALIG, LGALS2, LGALS3, Galactose-specific lectin 3, Mac-2 antigen, IgE-binding protein, 35 kDa lectin, Carbohydrate-binding protein 35, CBP 35, Laminin-binding protein, Lectin L-29, L-31, Galactoside-binding protein, GALBP.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Galectin-3 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Galectin-3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized LGALS3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MADNFSLHDAL SGSGNPNPQG WPGAWGNQPA GAGGYPGASY PGAYPGQAPP GAYPGQAPPG AYPGAPGAYP GAPAPGVYPG PPSGPGAYPS SGQPSATGAY PATGPYGAPA GPLIVPYNLP LPGGVVPRML ITILGTVKPN ANRIALDFQR GNDVAFHFNP RFNENNRRVI VCNTKLDNNW GREERQSVFP FESGKPFKIQ VLVEPDHFKV AVNDAHLLQY NHRVKKLNEI SKLGISGDID LTSASYTMI.
-
Background
What is the molecular weight/Mw of LGALS3 HUMAN Protein?
LGALS3 HUMAN Protein has a total Mw of 26.2kDa.
What is the source or expression system of LGALS3 HUMAN Protein?
Escherichia Coli.
What is the Purity of LGALS3 HUMAN Protein?
LGALS3 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS3 HUMAN Protein?
The biological functionality of LGALS3 HUMAN Protein will be determined in the future.
What is the amino acid sequence of LGALS3 HUMAN Protein?
MADNFSLHDAL SGSGNPNPQG WPGAWGNQPA GAGGYPGASY PGAYPGQAPP GAYPGQAPPG AYPGAPGAYP GAPAPGVYPG PPSGPGAYPS SGQPSATGAY PATGPYGAPA GPLIVPYNLP LPGGVVPRML ITILGTVKPN ANRIALDFQR GNDVAFHFNP RFNENNRRVI VCNTKLDNNW GREERQSVFP FESGKPFKIQ VLVEPDHFKV AVNDAHLLQY NHRVKKLNEI SKLGISGDID LTSASYTMI.
What applications can LGALS3 HUMAN Protein be used in?
LGALS3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS3 HUMAN Protein?
The endotoxin level is minimal, LGALS3 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 :
T.pallidum p47Description:
Treponema pallidum p47 Recombinant
Product # :
TRP-243Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
The E.Coli derived recombinant protein contains the T.Pallidum p47 immunodominant regions. The protein contains beta-galactosidase (114 kDa) fused at the N- terminus.
Source
Escherichia Coli.
Formulation
8M urea, 10mM Tris-HCl pH 8.0, 1mM EDTA and 1mM DTT.
Purity
Treponema Pallidum protein is >95% pure as determined by SDS-PAGE.
More Info
-
Introduction
Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum subsp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.
-
Stability
Treponema Pallidum although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Applications
Treponema Pallidum protein is suitable for ELISA and Western blots, excellent antigen for detection of T.Pallidum with minimal specificity problems.
-
Specificity
Immunoreactive with sera of T.Pallidum infected individuals.
-
Purification Method
Treponema Pallidum proteinwas purified by proprietary chromatographic technique.
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 :
P Selectin HumanDescription:
P-selectin Human Recombinant
P-selectin, Granule membrane protein 140, GMP-140, PADGEM, Leukocyte-endothelial cell adhesion molecule 3, LECAM3, CD62 antigen-like family member P, CD62P antigen, SELP, GMRP, GRMP, CD62, PSEL, CD62P, GMP140, FLJ45155.
Product # :
PRO-382Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
P-Selectin Human Recombinant is expressed in E. coli containing 566 amino acids 197-761 fused to an amino terminal hexahistidine tag.
Source
Escherichia Coli.
Formulation
P-Selectin is supplied in 50% Glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Single band on Western Blot.More Info
-
Introduction
P-Selectin also called Platelet Alpha-Granule Membrane Protein, CD62, and Granulocyte Membrane Protein GRMP belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. Pselectin is expressed transiently on the surface of activated platelets and endothelial cells. P-Selectin is a 140 kDa protein which is stored in the alpha-granules of platelets and Weibel-Palade bodies of endothelial cells. Secreted P-selectin is thought to play a key role in the adhesion of platelets to monocytes and neutrophils during an inflammatory response. P-Selectin is a calcium-dependent receptor that binds to sialylated forms of Lewis blood group carbohydrate antigens on neutrophils and monocytes. Levels of P-Selectin may be elevated in a number of pathological conditions.
-
Synonyms
P-selectin, Granule membrane protein 140, GMP-140, PADGEM, Leukocyte-endothelial cell adhesion molecule 3, LECAM3, CD62 antigen-like family member P, CD62P antigen, SELP, GMRP, GRMP, CD62, PSEL, CD62P, GMP140, FLJ45155.
-
Physical Appearance
Sterile Filtered liquid formulation.
-
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.
-
Applications
P-Selectin can be used directly as a positive control in Western blotting, ELISA, immunoprecipitation and other immunological experiments.
The biological activity of this product has not yet been tested.
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 :
MALD3Description:
Non-Specific Lipid-Transfer Protein Mal d 3 Recombinant
Non-specific lipid-transfer protein, LTP, MALD3.
Product # :
ALR-023Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Non-Specific Lipid-Transfer Protein Mal d 3 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 12kDa.MALD3 is expressed with a 6xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
MALD3 is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
MALD3 (a non-specific lipid transfer protein) is a major apple allergen. LTPs are found mainly in aerial plant organs such as leaves, seeds, flowers, and fruit. MALD3 is a heat-stable protein which is characterized by having resistance to pepsin hydrolysis.
-
Synonyms
Non-specific lipid-transfer protein, LTP, MALD3.
-
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.Avoid multiple freeze-thaw cycles.
-
Immunological Functions
1. Binds IgE-type human antibodies.2. Immunodot test with positive/negative samples
-
Applications
Tested by LAL (Limulus Amoebocyte Lysate) chromogenic endotoxin assay.
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.