Search: 1000 results found for "ephrin"

Description:

Egl Nine Homolog 3 Human Recombinant

Egl nine homolog 3 (C. elegans), Hypoxia-inducible factor prolyl hydroxylase 3, Prolyl hydroxylase domain-containing protein 3, HIF-PH3, PHD3, egl nine-like protein 3 isoform, HIF prolyl hydroxylase 3, EC 1.14.11.29, HPH-1, HPH-3.

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PRO-1143

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Description

EGLN3 Human Recombinant produced in E. coli is a single polypeptide chain containing 263 amino acids (1-239) and having a molecular mass of 29.8 kDa.EGLN3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The EGLN3 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 300mM NaCl, 5mM DTT, 2mM EDTA and 50% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Egl Nine Homolog 3 (EGLN3) belongs to the EGLN family of prolyl hydroxylases. EGLN3 catalyzes hydroxylation of the ? subunit of hypoxia-inducible factor-?, which targets hypoxia-inducible factor-? for ubiquitination by a ubiquitin ligase complex containing the von Hippel-Lindau (VHL) tumor suppressor. EGLN3 is the most significant isozyme in limiting physiological activation of HIFs (especially HIF2A) in hypoxia. EGLN3 is activated in cardiovascular cells and Hela cells after exposure to hypoxia. In addition, EGLN3 hydroxylates PKM2 in hypoxia, thus limiting glycolysis. Under normoxia, EGLN3 hydroxylates and regulates the stability of ADRB2. EGLN3 is inhibited by polynitrogen compounds possibly by chelation to Fe2+ ions.
Synonyms
Egl nine homolog 3 (C. elegans), Hypoxia-inducible factor prolyl hydroxylase 3, Prolyl hydroxylase domain-containing protein 3, HIF-PH3, PHD3, egl nine-like protein 3 isoform, HIF prolyl hydroxylase 3, EC 1.14.11.29, HPH-1, HPH-3.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMPLGHI MRLDLEKIAL EYIVPCLHEV GFCYLDNFLG EVVGDCVLER VKQLHCTGAL RDGQLAGPRA GVSKRHLRGD QITWIGGNEE GCEAISFLLS LIDRLVLYCG SRLGKYYVKE RSKAMVACYP GNGTGYVRHV DNPNGDGRCI TCIYYLNKNW DAKLHGGILR IFPEGKSFIA DVEPIFDRLL FFWSDRRNPH EVQPSYATRY AMTVWYFDAE ERAEAKKKFR NLTRKTESAL TED

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Pigment Epithelium-Derived Factor Human Recombinant, HEK

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

Product # :

CYT-553

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Description

PEDF Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain containing a total of 410 amino acids, having a molecular mass of 45.6 kDa and fused to an 11 aa FLAG tag at C-Terminus.The Human PEDF is purified by proprietary chromatographic techniques.

Source

HEK 293.

Formulation

The filtered (0.4µm) concentrated (0.5mg/ml) protein solution was lyophilized with 20mM Tris & 20mM NaCl pH-7.5.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
PEDF is a neurotrophic protein that induces extensive neuronal differentiation in retinoblastoma cells. SerpinF1 is a potent inhibitor of angiogenesis. EPC1 doesn’t undergo the stressed to relaxed conformation transition characteristic as of the active serpins since it exhibits no serine protease inhibitory activity.
Aqueous humour level of asymmetric dimethylarginine is correlated with PEDF in humans. ADMA and PEDF levels are increased in response to inflammation in uveitis.
Lack of PEDF expression is a potent factor for the enhancement of tumor growth and angiogenesis in breast cancer.
PEDF & VEGF genes contribute to the development of diabetic retinopathy.
PEDF and VEGF structural changes in blood vessel wall play an important role in the pathophysiology of PD patients.
PEDF-overexpressing tumors exhibited reduced intratumoral angiogenesis.
SerpinF1 is a new promising approach for the treatment of osteosarcoma.
Levels of the natural ocular anti-angiogenic factor SentrinF1 (PEDF) is associated with proliferative retinopathy.
VEGF secreted by retinal pigment epithelial cells upregulates PEDF expression via VEGFR-1 in an autocrine manner.
Sentrin-F1 concentration in the aqueous humor of diabetic patients predicts who will develop progression of retinopathy.
PEDF blocks angiogenic effects of leptin through its anti-oxidative properties.
Synonyms
Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
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 recomnded to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
QNPASPPEEG SPDPDSTGAL VEEEDPFFKV PVNKLAAAVS NFGYDLYRVR SSTSPTTNVL LSPLSVATAL SALSLGAEQR TESIIHRALY YDLISSPDIH GTYKELLDTV TAPQKNLKSA SRIVFEKKLR IKSSFVAPLE KSYGTRPRVL TGNPRLDLQE INNWVQAQMK GKLARSTKEI PDEISILLLG VAHFKGQWVT KFDSRKTSLE DFYLDEERTV RVPMMSDPKA VLRYGLDSDL SCKIAQLPLT GSMSIIFFLP LKVTQNLTLI EESLTSEFIH DIDRELKTVQ AVLTVPKLKL SYEGEVTKSL QEMKLQSLFD SPDFSKITGK PIKLTQVEHR AGFEWNEDGA GTTPSPGLQP AHLTFPLDYH LNQPFIFVLR DTDTGALLFI GKILDPRGPAAADYKDDDDK.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Laforin, Mouse Anti Human

Laforin, Lafora PTPase, LAFPTPase, EPM2A, EPM2, MELF, epilepsy progressive myoclonus type 2A Lafora disease.

Product # :

ANT-427

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Formulation

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

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Introduction
EPM2A is a dual-specificity phosphatase which associates with polyribosomes. The EPM2A protein may be involved in the regulation of glycogen metabolism. Mutations in the EPM2A gene have been linked to myoclonic epilepsy of Lafora.
Synonyms
Laforin, Lafora PTPase, LAFPTPase, EPM2A, EPM2, MELF, epilepsy progressive myoclonus type 2A Lafora disease.
Immunogen
Anti-human EPM2A mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human EPM2A amino acids 243-331 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
Clone
P3F3AT.
Applications
EPM2A antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1,000 ~ 2,000. Recommended starting dilution is 1:1,000.
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
EPM2A antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Holo Transferrin Human Recombinant

Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.

Product # :

PRO-2844

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sds-page, activity

Description

Human Holo Transferrin Recombinant produced in HEK Cells is a glycosylated polypeptide containing 679 amino acids and having a Mw of of 76 kDa.

Source

HEK Cells

Formulation

The protein was lyophilized from 1x PBS pH-7.4.

Purity

Protein is >98% pure as determined by 10% PAGE (coomassie staining).

Biological Activity

The activity of Recombinant Holo Transferrin was determined by the proliferation assay using MDCK cells stimulated with recombinant human Holo Transferrin. The protein was found biologically active

sds-page, activity

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Introduction
Recombinant Human Holo Transferrin is an iron-delivery signaling protein which functions in the delivery of Fe³⁺ iron to cells using transferrin receptor-1 (TfR1/CD71).
Holo-transferrin binds TfR1, undergoes receptor-mediated endocytosis and the iron is released intracellularly. Transferrin Human Recombinant is crucial for brain and the nervous system, neuronal mitochondrial metabolism, neurotransmitter synthesis, oligodendrocyte myelination and synaptic activity. Recombinant holo-transferrin can be used in cell therapy, stem-cell expansion, CHO production, or drug-delivery platforms.
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
Physical Appearance
Sterile Filtered lyophilized (freeze-dried) powder.
Stability
Store the lyophilized Holo Transferrin recombinant between 2-8°C, do not freeze.
Upon reconstitution Holo 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 recombinant in sterile 18MΩ-cm H2O at 1mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VPDKTVRWCA VSEHEATKCQ SFRDHMKSVI PSDGPSVACV KKASYLDCIR AIAANEADAV TLDAGLVYDA YLAPNNLKPV VAEFYGSKED PQTFYYAVAV VKKDSGFQMN QLRGKKSCHT GLGRSAGWNI PIGLLYCDLP EPRKPLEKAV ANFFSGSCAP CADGTDFPQL CQLCPGCGCS TLNQYFGYSG AFKCLKDGAG DVAFVKHSTI FENLANKADR DQYELLCLDN TRKPVDEYKD CHLAQVPSHT VVARSMGGKE DLIWELLNQA QEHFGKDKSK EFQLFSSPHG KDLLFKDSAH GFLKVPPRMD AKMYLGYEYV TAIRNLREGT CPEAPTDECK PVKWCALSHH ERLKCDEWSV NSVGKIECVS AETTEDCIAK IMNGEADAMS LDGGFVYIAG KCGLVPVLAE NYNKSDNCED TPEAGYFAVA VVKKSASDLT WDNLKGKKSC HTAVGRTAGW NIPMGLLYNK INHCRFDEFF SEGCAPGSKK DSSLCKLCMG SGLNLCEPNN KEGYYGYTGA FRCLVEKGDV AFVKHQTVPQ NTGGKNPDPW AKNLNEKDYE LLCLDGTRKP VEEYANCHLA RAPNHAVVTR KDKEACVHKI LRQQQHLFGS NVTDCSGNFC LFRSETKDLL FRDDTVCLAK LHDRNTYEKY LGEEYVKAVG NLRKCSTSSL LEACTFRRP.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Transferrin Human Recombinant, CHO

Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.

Product # :

PRO-2782

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Description

Recombinant Human Transferrin produced in CHO cells is a glycosylated, polypeptide chain containing having a molecular mass of 76 kDa. Human Transferrin has homologous C and N-terminal domains, each of which binds one ion of ferric iron.

Source

Chinese Hamster Ovary cells.

Formulation

Transferrin solution contains 0.05% NaN3 and PBS.

Purity

Protein is >95% pure as determined by 10% PAGE (coomassie staining).

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Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
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.
Applications
Immunoassay, cell culture.
Background
Human recombinant transferrin, a glycoprotein responsible for iron transport in the body, has gained increasing attention in the fields of biomedicine and health sciences. This multifaceted protein serves as an essential carrier of iron and is crucial for cellular growth, immunity, and various physiological processes. Its recombinant form, produced through advanced biotechnological methods, offers several advantages for therapeutic and research purposes. This study aims to provide a comprehensive exploration of human recombinant transferrin, shedding light on its various functions and potential applications in health and biomedicine.
The primary objective of this research is to elucidate the essential role of transferrin in iron homeostasis and its significance for human health. In vitro and in vivo experiments will be conducted to investigate how recombinant transferrin interacts with cellular receptors, regulates iron uptake, and influences cellular proliferation. Understanding these mechanisms is fundamental for deciphering the complexities of iron metabolism and its impact on health and disease.
The second objective is to assess the clinical relevance of human recombinant transferrin in medical interventions. Clinical trials and studies involving individuals with iron-related disorders, such as iron-deficiency anemia, will be conducted to evaluate the efficacy and safety of recombinant transferrin supplementation. These investigations may provide insights into the use of recombinant transferrin as a therapeutic agent in various clinical settings.
The third objective is to explore the broader implications of human recombinant transferrin in biomedicine and research. Research will investigate its potential roles in areas beyond iron transport, such as drug delivery, tissue engineering, and cell culture. Understanding the multifaceted properties of recombinant transferrin may open new avenues for innovative approaches in various medical specialties and scientific research.
By delving into the diverse functions of human recombinant transferrin, this research aims to expand our understanding of its physiological roles and clinical applications. The findings may contribute to the development of innovative strategies for the treatment of iron-related disorders and the advancement of biomedicine and scientific research.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Epithelial Cell Adhesion Molecule, Mouse Anti Human

Epithelial cell adhesion molecule, Ep-CAM, Adenocarcinoma-associated antigen, Cell surface glycoprotein Trop-1, Epithelial cell surface antigen, Epithelial glycoprotein, EGP, Epithelial glycoprotein 314, EGP314, hEGP314, KS 1/4 antigen, KSA, Major gastrointestinal tumor-associated protein GA733-2, Tumor-associated calcium signal transducer 1, CD326, EPCAM, GA733-2, M1S2, M4S1, MIC18, TACSTD1, TROP1, ESA, MK-1, DIAR5, EGP-2, EGP40, KS1/4, HNPCC8.

Product # :

ANT-525

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Formulation

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

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Introduction
EPCAM is a carcinoma-associated antigen and belongs to a family which includes at least 2 type I membrane proteins. The EPCAM protein has a role in embryonic stem cells proliferation and differentiation. EPCAM is used as a target for immunotherapy treatment of human carcinomas. EPCAM is expressed on most normal epithelial cells and gastrointestinal carcinomas and acts as a homotypic calcium-independent cell adhesion molecule. Epithelial cell adhesion molecules (EPCAM) can act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for supplying immunological barrier as a first line of defense against mucosal infection. EPCAM gene mutations result in congenital tufting enteropathy.
Synonyms
Epithelial cell adhesion molecule, Ep-CAM, Adenocarcinoma-associated antigen, Cell surface glycoprotein Trop-1, Epithelial cell surface antigen, Epithelial glycoprotein, EGP, Epithelial glycoprotein 314, EGP314, hEGP314, KS 1/4 antigen, KSA, Major gastrointestinal tumor-associated protein GA733-2, Tumor-associated calcium signal transducer 1, CD326, EPCAM, GA733-2, M1S2, M4S1, MIC18, TACSTD1, TROP1, ESA, MK-1, DIAR5, EGP-2, EGP40, KS1/4, HNPCC8.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human EPCAM mAb, clone PAT37F9AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human EPCAM protein 24-265 amino acids purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
Clone
PAT36F10AT.
Applications
The 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 1:500.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
EPCAM 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.

Description:

Epidermal Growth Factor Long Human Recombinant

Urogastrone, URG, EGF.

Product # :

CYT-798

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Description

Recombinant Human EGF Long produced in E.coli cells is a single non-glycosylated, polypeptide chain containing 106 amino acids and having a molecular mass of 12.3kDa. The EGF Long is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The EGF Long was lyophilized from a 0.2µm filtered concentrated solution in 10mM HCl.

Purity

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

Biological Activity

The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 10⁶ IU/mg.

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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. Long EGF is a recombinant analog of Human EGF developed as a replacement for use in therapeutic cell culture applications as a like-for-like supplement for Recombinant Human or native EGF. It includes the Human EGF amino acid sequence plus a 53 amino acid N-terminal extension peptide.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized EGF Long although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF Long 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 EGF Long in sterile 100mM AcOH (acetic Acid) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MFPAMPLSSL FANAVLRAQH LHQLAADTYK EFERAYIPEG QRYSIQVNFA HYGNSDSECP LSHDGYCLHD GVCMYIEALD KYACNCVVGY IGERCQYRDL KWWELR
Background
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 12.3kDa.

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

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

What is the Biological Activity of EGF Protein?
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 106 IU/mg.

What is the amino acid sequence of EGF Protein?
MFPAMPLSSL FANAVLRAQH LHQLAADTYK EFERAYIPEG QRYSIQVNFA HYGNSDSECP LSHDGYCLHD GVCMYIEALD KYACNCVVGY IGERCQYRDL KWWELR

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.

Description:

Leuprolide Human

Leuprolide, Leuprorelin.

Product # :

HOR-260

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Description

Leuprolide Human Synthetic is a single, non-glycosylated, polypeptide chain containing 9 amino acids and having a molecular mass of 1209 Dalton. The molecular formula is C59H84N16O12.

Formulation

The Leuprorelin was lyophilized from a concentrated (1mg/ml) solution with no additives.

Purity

Greater than 98.0% as determined by RP-HPLC.

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Introduction
Leuprorelin (INN) or leuprolide acetate (USAN) is a gonadotropin-releasing hormone agonist (GnRH agonist).
By causing constant stimulation of the pituitaryGnRH receptors, it initially causes stimulation (flare), but thereafter decreases pituitary secretion (downregulation) of gonadotropins luteinizing hormone(LH) and follicle-stimulating hormone(FSH).
Like other GnRH agonists, leuprolide may be used in the treatment of hormone-responsive cancers such as prostate canceror breast cancer, estrogen-dependent conditions (such as endometriosisor uterine fibroids), to treat precocious puberty, and to control ovarian stimulation in IVF.
Synonyms
Leuprolide, Leuprorelin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leoprolide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leuprorelin 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 Leoprolide in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
pGlu-His-Trp-Ser-Tyr-D-Leu-Leu-Arg-Pro-NHEt.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Proheparin-Binding EGF-like Growth Factor Rat Recombinant

Proheparin-binding EGF-like growth factor, Heparin-binding EGF-like growth factor, HB-EGF, HBEGF, Dtr, Hegfl, GFHB.

Product # :

CYT-170

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Description

HB-EGF Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids and having a molecular mass of 9.7kDa.The HB-EGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was filtered (0.2µm) and lyophilized from a concentrated solution containing PBS, 300mM NaCl, pH 7.4 and 5% trehalose.

Purity

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

Biological Activity

The ED₅₀ as determined by a cell proliferation assay using balb/c 3T3 cells is < 1.0 ng/ml, corresponding to a specific activity of > 1.0×10⁶ units/mg.

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Introduction
HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC (smooth muscle cells), fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind heparin and heparin sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.
Synonyms
Proheparin-binding EGF-like growth factor, Heparin-binding EGF-like growth factor, HB-EGF, HBEGF, Dtr, Hegfl, GFHB.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Rat HB-EGF Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HB-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 Rat HB-EGF in sterile 18M-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DLEGTDLDLF KVAFSSKPQA LATPGKEKNG KKKRKGKGLG KKRDPCLKKY KDYCIHGECR YLKELRIPSC HCLPGYHGQR CHGLTL.
Background
What is the molecular weight/Mw of HB-EGF Protein?
HB-EGF Protein has a total Mw of 9.7kDa.

What is the source or expression system of HB-EGF Protein?
Escherichia Coli.

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

What is the Biological Activity of HB-EGF Protein?
The ED50 as determined by a cell proliferation assay using balb/c 3T3 cells is < 1.0 ng/ml, corresponding to a specific activity of > 1.0×106 units/mg.

What is the amino acid sequence of HB-EGF Protein?
DLEGTDLDLF KVAFSSKPQA LATPGKEKNG KKKRKGKGLG KKRDPCLKKY KDYCIHGECR YLKELRIPSC HCLPGYHGQR CHGLTL.

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

What is the endotoxin level for HB-EGF Protein?
The endotoxin level is minimal, HB-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.

Description:

Apolipoprotein-J Mouse Recombinant

CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.

Product # :

CYT-1172

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Description

Clusterin Mouse Recombinant is a single, glycosylated polypeptide chain containing 433 amino acids (22-448a.a) and having a molecular mass of 50.2kDa (calculated). Clusterin is fused to a 6 a.a His tag at C-terminal.

Source

HEK293

Formulation

Clusterin filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20 mM Tris buffer and 50 mM NaCl, pH 7.5.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Clusterin also known as Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by 5 disulfide bridges and are flanked by 2 predicted coiled-coil a-helices and 3 predicted amphipathic a-helices.
Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% -80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
Clusterin is up/down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.
Synonyms
CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.
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
EQEVSDNELQ ELSTQGSRYI NKEIQNAVQG VKHIKTLIEK TNAERKSLLN SLEEAKKKKE DALEDTRDSE MKLKAFPEVC NETMMALWEE CKPCLKHTCM KFYARVCRSG SGLVGQQLEE FLNQSSPFYF WMNGDRIDSL LESDRQQSQV LDAMQDSFAR ASGIIDTLFQ DRFFARELHD PHYFSPIGFP HKRPHFLYPK SRLVRSLMSP SHYGPPSFHN MFQPFFEMIH QAQQAMDVQL HSPAFQFPDV DFLREGEDDR TVCKEIRRNS TGCLKMKGQC EKCQEILSVD CSTNNPAQAN LRQELNDSLQ VAERLTEQYK ELLQSFQSKM LNTSSLLEQL NDQFNWVSQL ANLTQGEDKY YLRVSTVTTH SSDSEVPSRV TEVVVKLFDS DPITVVLPEE VSKDNPKFMD TVAEKALQEY RRKSRAEHHH HHH
Background
What is the molecular weight/Mw of CLUSTERIN Protein?
CLUSTERIN Protein has a total Mw of 50.2kDa.

What is the source or expression system of CLUSTERIN Protein?
HEK293

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

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

What is the amino acid sequence of CLUSTERIN Protein?
EQEVSDNELQ ELSTQGSRYI NKEIQNAVQG VKHIKTLIEK TNAERKSLLN SLEEAKKKKE DALEDTRDSE MKLKAFPEVC NETMMALWEE CKPCLKHTCM KFYARVCRSG SGLVGQQLEE FLNQSSPFYF WMNGDRIDSL LESDRQQSQV LDAMQDSFAR ASGIIDTLFQ DRFFARELHD PHYFSPIGFP HKRPHFLYPK SRLVRSLMSP SHYGPPSFHN MFQPFFEMIH QAQQAMDVQL HSPAFQFPDV DFLREGEDDR TVCKEIRRNS TGCLKMKGQC EKCQEILSVD CSTNNPAQAN LRQELNDSLQ VAERLTEQYK ELLQSFQSKM LNTSSLLEQL NDQFNWVSQL ANLTQGEDKY YLRVSTVTTH SSDSEVPSRV TEVVVKLFDS DPITVVLPEE VSKDNPKFMD TVAEKALQEY RRKSRAEHHH HHH

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

What is the endotoxin level for CLUSTERIN Protein?
The endotoxin level is minimal, CLUSTERIN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Osteocrin Human Recombinant, HEK

Osteocrin, Musclin, OSTN.

Product # :

PRO-2818

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Description

Osteocrin Human Recombinant is a single, glycosylated, polypeptide chain (28-133 a.a) containing a total of 112 amino acids and having a molecular mass of 12.5 kDa. Osteocrin is fused to a 6 a.a His-Tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The Osteocrin solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 range ≤ 20 ng/ml measured by its binding ability in a functional ELISA with Human NPRC.

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Synonyms
Osteocrin, Musclin, OSTN.
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
VDVTTTEAFD SGVIDVQSTP TVREEKSATD LTAKLLLLDE LVSLENDVIE TKKKRSFSGF GSPLDRLSAG SVDHKGKQRK VVDHPKRRFG IPMDRIGRNR LSNSRGHHHH HH.
Background
Research has demonstrated that osteocrin influences bone formation by enhancing the anabolic effects of osteoblasts, the cells responsible for new bone formation. In addition to its skeletal roles, osteocrin has been shown to regulate cardiovascular functions by modulating blood pressure and cardiac hypertrophy. Furthermore, emerging evidence suggests that osteocrin may play a role in the central nervous system, impacting cognitive function and neuroprotection.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

GDP Dissociation Inhibitor 2 Human Recombinant

GDP Dissociation Inhibitor 2, GDI2, RABGDIB, Guanosine Diphosphate Dissociation Inhibitor 2 , Rab GDI Beta , GDI-2, Epididymis Secretory Sperm Binding Protein Li 46e, Rab GDP Dissociation Inhibitor Beta , Rab GDP-Dissociation , HEL-S-46e.

Product # :

PRO-1948

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Description

GDI2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 468 amino acids (1-445) and having a molecular mass of 53.1 kDa.GDI2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GDI2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Rab GDP dissociation inhibitor beta isoform 1 (GDI2) is a member of the GDP dissociation inhibitors (GDIs) family. GDI proteins can bind and release GDP-bound Rab proteins from membranes. GDI1 interacts with virtually all of the Rab proteins, whereas GDI2 interacts with Rabll but not Rab3A. GDI2 distributes ubiquitously, presenting a membrane bound location in perinuclear regions of cells.
Synonyms
GDP Dissociation Inhibitor 2, GDI2, RABGDIB, Guanosine Diphosphate Dissociation Inhibitor 2 , Rab GDI Beta , GDI-2, Epididymis Secretory Sperm Binding Protein Li 46e, Rab GDP Dissociation Inhibitor Beta , Rab GDP-Dissociation , HEL-S-46e.
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 MGSMNEEYDV IVLGTGLTEC ILSGIMSVNG KKVLHMDRNP YYGGESASIT PLEDLYKRFK IPGSPPESMG RGRDWNVDLI PKFLMANGQL VKMLLYTEVT RYLDFKVTEG SFVYKGGKIY KVPSTEAEAL ASSLMGLFEK RRFRKFLVYV ANFDEKDPRT FEGIDPKKTT MRDVYKKFDL GQDVIDFTGH ALALYRTDDY LDQPCYETIN RIKLYSESLA RYGKSPYLYP LYGLGELPQG FARLSAIYGG TYMLNKPIEE IIVQNGKVIG VKSEGEIARC KQLICDPSYV KDRVEKVGQV IRVICILSHP IKNTNDANSC QIIIPQNQVN RKSDIYVCMI SFAHNVAAQG KYIAIVSTTV ETKEPEKEIR PALELLEPIE QKFVSISDLL VPKDLGTESQ IFISRTYDAT THFETTCDDI KNIYKRMTGS EFDFEEMKRK KNDIYGED.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Eukaryotic Translation Initiation Factor 2 Subunit 1 Alpha, Mouse Anti Human

Eukaryotic translation initiation factor 2 subunit 1, Eukaryotic translation initiation factor 2 subunit alpha, eIF-2-alpha, EIF-2alpha, EIF-2A, EIF2, EIF-2, EIF2A, EIF-2A.

Product # :

ANT-059

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formulation
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Formulation

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

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Introduction
EIF2S1 participates in the premature steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA which binds to a 40S ribosomal subunit, followed by mRNA binding to create a 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 should exchange with GTP by way of a reaction catalyzed by eIF-2B.
Synonyms
Eukaryotic translation initiation factor 2 subunit 1, Eukaryotic translation initiation factor 2 subunit alpha, eIF-2-alpha, EIF-2alpha, EIF-2A, EIF2, EIF-2, EIF2A, EIF-2A.
Immunogen
Anti-human EIF2S1 mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human EIF2S1 amino acids 1-315 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and kappa light chain.
Clone
PEIF2S1AT.
Applications
EIF2S1 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Recommended dilution range for Western blot analysis is 1:1,000.
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
EIF2S1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Endothelial Cell-Specific Molecule 1 Human Recombinant, HEK

Endothelial cell-specific molecule 1, ESM-1, ESM1, endocan.

Product # :

PRO-2476

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Description

ESM1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 20-184) containing 175 amino acids including a 10 a.a C-terminal His tag. The total molecular mass is 19.5kDa (calculated).

Source

HEK293 cells.

Formulation

ESM1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Endothelial cell-specific molecule 1 (ESM1) is a proteoglycan secreted by endothelial cells (mostly in the human lung and kidney tissues) and its mRNA expression is regulated by inflammatory cytokines. ESM1 has potent implications in lung endothelial cell-leukocyte interactions. In addition, ESM1 expression is detected in various epithelia and in adipocytes. ESM1 is involved in angiogenesis and it also promotes angiogenic sprouting. ESM1 expression is upregulated by TNF alpha, IL1 beta, or lipopolysaccharide and downregulated by IFN gamma. Genetically engineered cells overexpressing ESM1 induce tumor formation, implying that ESM1 might be involved in the pathophysiology of tumor growth in vivo.
Synonyms
Endothelial cell-specific molecule 1, ESM-1, ESM1, endocan.
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. ESM1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
WSNNYAVDCP QHCDSSECKS SPRCKRTVLD DCGCCRVCAA GRGETCYRTV SGMDGMKCGP GLRCQPSNGE DPFGEEFGIC KDCPYGTFGM DCRETCNCQS GICDRGTGKC LKFPFFQYSV TKSSNRFVSL TEHDMASGDG NIVREEVVKE NAAGSPVMRK WLNPR HHHHH HHHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Epithelial Cell Adhesion Molecule Human Recombinant, Sf9

Epithelial Cell Adhesion Molecule , Tumor-Associated Calcium Signal Transducer 1, Major Gastrointestinal Tumor-Associated Protein GA733-2, Adenocarcinoma-Associated Antigen, Cell Surface Glycoprotein Trop-1, Epithelial Glycoprotein 314, TACSTD1, EGP314, MIC18, TROP1, M4S1, KSA, Membrane Component, Chromosome 4, Surface Marker (35kD Glycoprotein), Antigen Identified By Monoclonal Antibody AUA1, Human Epithelial Glycoprotein-2, Epithelial Cell Surface Antigen, Epithelial Glycoprotein, KS 1/4 Antigen, CD326 Antigen, GA733-2, HEGP314, HNPCC8, Ep-CAM, DIAR5, EGP-2, EGP40, KS1/4, MK-1, M1S2, ESA, EGP, EPCAM.

Product # :

PRO-2238

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Description

EPCAM produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (24-265 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 248 amino acids and having a molecular mass of 28.2kDa.EPCAM shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

EPCAM protein solution (1mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
EPCAM is a carcinoma-associated antigen and belongs to a family which includes at least 2 type I membrane proteins. The EPCAM protein has a role in embryonic stem cells proliferation and differentiation. EPCAM is used as a target for immunotherapy treatment of human carcinomas. EPCAM is expressed on most normal epithelial cells and gastrointestinal carcinomas and acts as a homotypic calcium-independent cell adhesion molecule. Epithelial cell adhesion molecules (EPCAM) can act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for supplying immunological barrier as a first line of defense against mucosal infection. EPCAM gene mutations result in congenital tufting enteropathy.
Synonyms
Epithelial Cell Adhesion Molecule , Tumor-Associated Calcium Signal Transducer 1, Major Gastrointestinal Tumor-Associated Protein GA733-2, Adenocarcinoma-Associated Antigen, Cell Surface Glycoprotein Trop-1, Epithelial Glycoprotein 314, TACSTD1, EGP314, MIC18, TROP1, M4S1, KSA, Membrane Component, Chromosome 4, Surface Marker (35kD Glycoprotein), Antigen Identified By Monoclonal Antibody AUA1, Human Epithelial Glycoprotein-2, Epithelial Cell Surface Antigen, Epithelial Glycoprotein, KS 1/4 Antigen, CD326 Antigen, GA733-2, HEGP314, HNPCC8, Ep-CAM, DIAR5, EGP-2, EGP40, KS1/4, MK-1, M1S2, ESA, EGP, EPCAM.
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
QEECVCENYK LAVNCFVNNN RQCQCTSVGA QNTVICSKLA AKCLVMKAEM NGSKLGRRAK PEGALQNNDG LYDPDCDESG LFKAKQCNGT STCWCVNTAG VRRTDKDTEI TCSERVRTYW IIIELKHKAR EKPYDSKSLR TALQKEITTR YQLDPKFITS ILYENNVITI DLVQNSSQKT QNDVDIADVA YYFEKDVKGE SLFHSKKMDL TVNGEQLDLD PGQTLIYYVD EKAPEFSMQG LKHHHHHH

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Desmopressin

Product # :

HOR-270

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Description

Desmopressin also called ADH (Anti-Diuretic Hormone) has a molecular formula of C46H64N14O12S2 , Mpr-Tyr-Phe-Gln-Asn-Cys-Pro-D-Arg-Gly-NH2 having a Mw of 1069.23 Dalton.

Formulation

The Desmopressin peptide was lyophilized with no additives.

Purity

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

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Introduction
Desmopressin is the first vasopressin analog with a very high and very specific antidiuretic effect, has been widely used for different therapeutic purposes and is believed to be partly responsible for the formation of memories learning and memory processes. Desmopressin increases urine concentration and decreases urine production. Desmopressin is used to prevent and control excessive thirst, urination, and dehydration.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Desmopressin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DDAVP 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 DDAVP 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.

Description:

Apolipoprotein-D Human Recombinant, HEK

Apolipoprotein D, Apo-D, ApoD.

Product # :

CYT-768

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Description

Apolipoprotein-D Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (aa 21-189) containing a total of 175 amino acids, having a molecular mass of 20.1kDa (calculated) and fused to a 6 aa His tag at C-Terminus.The Human APOD is purified by proprietary chromatographic techniques.

Source

HEK 293.

Formulation

Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Apolipoprotein-D is mainly associated with high density lipoproteins in human plasma. Apolipoprotein-D is an atypical apolipoprotein and, based on its primary structure, Apolipoprotein-D is a member of the lipocalin family. Lipocalins adopt a beta-barrel tertiary structure and transport small hydrophobic ligands. Apolipoprotein-D binds cholesterol, progesterone, pregnenolone, bilirubin and arachidonic acid.
Apolipoprotein-D is expressed in numerous tissues having high levels of expression in spleen, testes and brain. Apolipoprotein-D is present at high concentrations in the cyst fluid of women with gross cystic disease of the breast, a condition associated with increased risk of breast cancer. Apolipoprotein-D accumulates in regenerating peripheral nerves and in the cerebrospinal fluid of patients with neurodegenerative conditions, such as Alzheimer's disease. Apolipoprotein-D participates in maintenance and repair within the central and peripheral nervous systems. Apolipoprotein-D is a multi-ligand, multi-functional transporter and transports a ligand from 1 cell to another within an organ, scavenge a ligand within an organ for transport to the blood or could transport a ligand from the circulation to specific cells within a tissue.
Synonyms
Apolipoprotein D, Apo-D, ApoD.
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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
QAFHLGKCPN PPVQENFDVN KYLGRWYEIE KIPTTFENGR CIQANYSLME NGKIKVLNQE LRADGTVNQI EGEATPVNLT EPAKLEVKFS WFMPSAPYWI LATDYENYAL VYSCTCIIQL FHVDFAWILA RNPNLPPETV DSLKNILTSN NIDVKKMTVT DQVNCPKLSH HHHHH.
Background
What is the molecular weight/Mw of APO D Protein?
APO D Protein has a total Mw of 20.1kDa.

What is the source or expression system of APO D Protein?
HEK 293.

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

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

What is the amino acid sequence of APO D Protein?
QAFHLGKCPN PPVQENFDVN KYLGRWYEIE KIPTTFENGR CIQANYSLME NGKIKVLNQE LRADGTVNQI EGEATPVNLT EPAKLEVKFS WFMPSAPYWI LATDYENYAL VYSCTCIIQL FHVDFAWILA RNPNLPPETV DSLKNILTSN NIDVKKMTVT DQVNCPKLSH HHHHH.

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

What is the endotoxin level for APO D Protein?
The endotoxin level is minimal, APO D Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

E-selectin Human Recombinant

E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.

Product # :

PRO-380

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Description

E-Selectin Human Recombinant is expressed in E. coli containing amino acids 179-557 fused to an amino terminal hexahistidine tag, having a total molecular weight of 45.22 kDa.

Source

Escherichia Coli.

Formulation

E-Selectin is supplied in 1x PBS and 50% Glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.
Single band on Western Blot.

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Introduction
E-selectin which is also called Endothelial leukocyte adhesion molecule 1, ELAM1, ELAM belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. Eselectin is expressed on the surface of endothelial cells and mediates the interaction of leukocytes and platelets with endothelial cells during an inflammatory response. E-selectin is present in single copy in the human genome and contains 14 exons spanning about 13 kb of DNA.
Synonyms
E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.
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.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Eukaryotic Translation Initiation Factor 3F Human Recombinant

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

Product # :

PRO-1722

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Description

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

Source

Escherichia Coli.

Formulation

EIF3F protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, and 0.4M urea.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Eukaryotic Translation Initiation Factor 3F, also known as EIF3F belongs to the eIF-3 subunit F family. EIF3F is a component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which isessential for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosomeand facilitates the recruitment of eIF-1, eIF-1A, eIF 2: GTP: methionyl-tRNAi and eIF-5 to form the 43S preinitiationcomplex (43S PIC). In addition, the eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA forAUG recognition. The eIF-3 complex is also necessary for disassembly and recycling of post termination ribosomalcomplexes and subsequently prevents premature union of the 40S and 60S ribosomal subunits prior to initiation. Among the diseases associated with EIF3F are intrahepatic cholangiocarcinoma, and cholangiocarcinoma.
Synonyms
Eukaryotic Translation Initiation Factor 3, Subunit F, EIF3S5 , Eukaryotic Translation Initiation Factor 3, Subunit 5 (Epsilon, 47kD), EC 3.4.19.12, Deubiquitinating Enzyme EIF3f, eIF3f, eIF-3-epsilon, EIF3 P47, Eukaryotic Translation Initiation Factor 3 Subunit 5, eIF3-p47, Eukaryotic Translation Initiation Factor 3, Subunit 5 Epsilon, 47kDa.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMATPAVP VSAPPATPTP VPAAAPASVP APTPAPAAAP VPAAAPASSS DPAAAAAATA APGQTPASAQ APAQTPAPAL PGPALPGPFP GGRVVRLHPV ILASIVDSYE RRNEGAARVI GTLLGTVDKH SVEVTNCFSV PHNESEDEVA VDMEFAKNMY ELHKKVSPNE LILGWYATGH DITEHSVLIH EYYSREAPNP IHLTVDTSLQ NGRMSIKAYV STLMGVPGRT MGVMFTPLTV KYAYYDTERI GVDLIMKTCF SPNRVIGLSS DLQQVGGASA RIQDALSTVL QYAEDVLSGK VSADNTVGRF LMSLVNQVPK IVPDDFETML NSNINDLLMV TYLANLTQSQ IALNEKLVNL.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibronectin Type III And Ankyrin Repeat Domains 1 Human Recombinant

Fibronectin Type 3 And Ankyrin Repeat Domains 1, 1700007B22Rik.

Product # :

PRO-1768

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Description

FANK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 368 amino acids (1-345 a.a) and having a molecular mass of 40.7kDa.FANK1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FANK1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT, 0.1mM PMSF and 20% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
FANK1 was localized in the nuclei of identical cells in the seminiferous epithelium. Depending on its nuclear localization, a gene ontology analysis proposes that FANK1 has a DNA binding activity therefor operates as a transcription factor. The extremely controlled expression of FANK1, suggests that it takes part in regulating gene expression in the transition from the meiotic phase to the haploid phase throughout spermatogenesis.
Synonyms
Fibronectin Type 3 And Ankyrin Repeat Domains 1, 1700007B22Rik.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMEPQKIM PPSKPHPPVV GKVTHHSIEL YWDLEKKAKR QGPQEQWFRF SIEEEDPKMH TYGIIYTGYA TKHVVEGLEP RTLYRFRLKV TSPSGECEYS PLVSVSTTRE PISSEHLHRA VSVNDEDLLV RILQGGRVKV DVPNKFGFTA LMVAAQKGYT RLVKILVSNG TDVNLKNGSG KDSLMLACYA GHLDVVKYLR RHGASWQARD LGGCTALHWA ADGGHCSVIE WMIKDGCEVD VVDTGSGWTP LMRVSAVSGN QRVASLLIDA GANVNVKDRN GKTPLMVAVL NNHEELVQLL LDKGADASVK NEFGKGVLEM ARVFDRQSVV SLLEERKKKQ RPKKSCVC

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Epidermal Growth Factor, His Active Mouse Recombinant

AI790464, Pro-epidermal growth factor, URG.

Product # :

CYT-1054

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SDS-PAGE

Description

EGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids (977-1029 a.a) and having a molecular mass of 8.6kDa.EGF is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

EGF protein solution (0.25mg/ml) contains 10% glycerol, 20mM Tris-HCl (pH 8.0), 0.1M NaCl & 2mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using mouse Balb/3T3 cell. The ED50 for this effect less or equal to 1ng/ml.

SDS-PAGE

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Introduction
Pro-Epidermal Growth Factor Isoform 1 or EGF, is a globular peptide (77aa residues) which includes three intra molecular disulfide bonds. This protein acts as a growth factor that mediates the growth and proliferation of different epithelial & epidermal cells. Among other processes that EGF is part of are inhibition of gastric secretion and wound healing. EGF is a ligand for class I tyrosine kinase receptor (c-erbB).
Synonyms
AI790464, Pro-epidermal growth factor, URG.
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 MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.
Background
Deciphering Epidermal Growth Factor Signaling: Unveiling the Potential of His-Tagged Active Mouse Recombinant
Abstract:
This research paper delves into the intricate realm of Epidermal Growth Factor (EGF) signaling, focusing on the novel application of Histidine (His)-tagged Active Mouse Recombinant EGF. By employing sophisticated methodologies encompassing protein engineering, receptor binding assays, and cellular response analyses, this study sheds light on the multifaceted molecular attributes and therapeutic prospects of this innovative variant.
Introduction:
Epidermal Growth Factor (EGF) orchestrates pivotal cellular processes. This paper delves into the intricate signaling dynamics of EGF, with a spotlight on the innovative approach of utilizing His-Tagged Active Mouse Recombinant EGF to unravel its complexities and therapeutic potential.
Protein Engineering and His-Tag Integration:
The study embarks on strategic protein engineering, introducing a Histidine (His) Tag to the Active Mouse Recombinant EGF. This His-Tag facilitates purification and subsequent analyses, enabling a comprehensive exploration of EGF signaling.
Receptor Binding Assays and Ligand Interaction:
Advanced receptor binding assays unravel the nuances of EGF's interaction with its cognate receptor, including affinities and kinetics. By employing His-Tagged EGF, the study dissects the impact of the tag on receptor binding, shedding light on its potential implications on downstream signaling.
Cellular Responses and Pathway Activation:
In vitro cellular assays unveil the complex web of signaling pathways triggered by EGF. The study employs high-throughput techniques to investigate the intricate cascades initiated by His-Tagged Active Mouse Recombinant EGF, providing insights into its potential role in cell proliferation, migration, and survival.
Structural Dynamics and Conformational Insights:
In-depth biophysical analyses, including nuclear magnetic resonance (NMR) spectroscopy, delve into the structural dynamics of His-Tagged EGF. This sheds light on potential conformational changes induced by the tag and their impact on receptor binding affinity.
Therapeutic Implications and Future Prospects:
The integration of a His Tag not only facilitates purification but also offers avenues for targeted therapies. His-Tagged EGF could serve as a platform for tailored drug delivery, enhancing the precision of interventions in various pathologies.
Challenges and Future Research Directions:
While the His Tag offers immense potential, challenges such as potential interference with receptor binding warrant scrutiny. Future research should focus on optimizing the positioning of the tag and exploring its impact on downstream signaling cascades.
Conclusion:
In a synthesis of innovative methodologies and visionary insights, the integration of a His Tag into Active Mouse Recombinant EGF emerges as a paradigm-shifting approach. This technique not only enriches our understanding of EGF signaling dynamics but also presents exciting prospects for personalized therapeutic interventions.
What is the molecular weight/Mw of EGF MOUSE, HIS ACTIVE Protein?
EGF MOUSE, HIS ACTIVE Protein has a total Mw of 8.6kDa.

What is the source or expression system of EGF MOUSE, HIS ACTIVE Protein?
Escherichia Coli.

What is the Purity of EGF MOUSE, HIS ACTIVE Protein?
EGF MOUSE, HIS ACTIVE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of EGF MOUSE, HIS ACTIVE Protein?
Measured in a cell proliferation assay using mouse Balb/3T3 cell. The ED50 for this effect less or equal to 1ng/ml.

What is the amino acid sequence of EGF MOUSE, HIS ACTIVE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.
What applications can EGF MOUSE, HIS ACTIVE Protein be used in?
EGF MOUSE, HIS ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EGF MOUSE, HIS ACTIVE Protein?
The endotoxin level is minimal, EGF MOUSE, HIS ACTIVE Protein was purified using conventional chromatography techniques..

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibronectin Leucine Rich Transmembrane Protein 3 Human Recombinant, HEK

Fibronectin Leucine Rich Transmembrane Protein 3, Fibronectin-Like Domain, Containing Leucine-Rich Transmembrane Protein 3, HH21, Leucine-Rich Repeat, Transmembrane Protein FLRT3, KIAA1469.

Product # :

PRO-2805

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Description

FLRT3 Human Recombinant is a single, glycosylated, polypeptide chain (29-528 a.a) containing a total of 506 amino acids and having a molecular mass of 57.3 kDa. FLRT3 is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

FLRT3 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

>40%. Measured by the ability of the immobilized protein to support the adhesion of Neuro-2a neuroblast cells. When cells are added to human FLRT3 coated plates 5 ug/ml.

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Synonyms
Fibronectin Leucine Rich Transmembrane Protein 3, Fibronectin-Like Domain, Containing Leucine-Rich Transmembrane Protein 3, HH21, Leucine-Rich Repeat, Transmembrane Protein FLRT3, KIAA1469.
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
KSCPSVCRCD AGFIYCNDRF LTSIPTGIPE DATTLYLQNN QINNAGIPSD LKNLLKVERI YLYHNSLDEF PTNLPKYVKE LHLQENNIRT ITYDSLSKIP YLEELHLDDN SVSAVSIEEG AFRDSNYLRL LFLSRNHLST IPWGLPRTIE ELRLDDNRIS TISSPSLQGL TSLKRLVLDG NLLNNHGLGD KVFFNLVNLT ELSLVRNSLT AAPVNLPGTN LRKLYLQDNH INRVPPNAFS
YLRQLYRLDM SNNNLSNLPQ GIFDDLDNIT QLILRNNPWY CGCKMKWVRD WLQSLPVKVN VRGLMCQAPE KVRGMAIKDL NAELFDCKDS GIVSTIQITT AIPNTVYPAQ GQWPAPVTKQ PDIKNPKLTK DHQTTGSPSR KTITITVKSV TSDTIHISWK LALPMTALRL SWLKLGHSPA FGSITETIVT GERSEYLVTA LEPDSPYKVC MVPMETSNLY LFDETPVCIE TETAPLRMYN
PTTTLNREQE KEPYKNPNLP HHHHHH.
Background
Fibronectin leucine-rich transmembrane protein 3, commonly known as FLRT3, stands as a molecular architect in the intricate landscape of neural development. Its roles, initially discovered in the embryonic nervous system, have expanded to encompass various physiological and pathological processes in both the brain and beyond. This research endeavors to unravel the enigma of FLRT3 protein, exploring its structural intricacies, physiological functions, and its far-reaching implications in neurobiology, embryogenesis, and disease. By delving into FLRT3's multifaceted roles, scientists aim to decipher the underlying mechanisms that govern its diverse functions and explore potential therapeutic avenues in the realms of neuroscience and beyond.
Structural Complexities of FLRT3:
FLRT3 belongs to the FLRT family, characterized by extracellular leucine-rich repeats (LRRs) and a transmembrane domain. These structural motifs enable FLRT3 to participate in a myriad of interactions, including binding with cell adhesion molecules and guidance cues. Understanding the three-dimensional architecture of FLRT3 is fundamental for unraveling its molecular partnerships, biological activities, and its contributions to cell adhesion and signaling.
Physiological Functions in Neural Development:
In the developing nervous system, FLRT3 acts as a guidance molecule, steering growing axons and dendrites to their precise destinations. Through interactions with other cell surface receptors and ligands, FLRT3 modulates axon pathfinding, synapse formation, and neuronal migration. Its presence in growth cones and developing neural circuits underscores its significance in sculpting the intricate neural networks essential for proper brain function.
Beyond Neural Development:
Beyond its canonical roles in neurodevelopment, FLRT3 has emerged as a versatile player in various physiological processes. It participates in tissue morphogenesis, modulates cell adhesion, and influences immune responses. Recent studies have also implicated FLRT3 in cancer progression, highlighting its involvement in pathological conditions and making it a potential target for therapeutic interventions in cancer therapy.
FLRT3 as a Therapeutic Target:
The diverse roles of FLRT3 in neural development and diseases position it as an attractive target for therapeutic interventions. Modulating FLRT3 interactions offers novel avenues for neurological disorder treatments, including neurodevelopmental disorders and neurodegenerative diseases. Moreover, understanding FLRT3's involvement in cancer biology opens doors for innovative cancer therapies, making it a promising target for precision medicine approaches.
FLRT3, with its intricate structural features and diverse functional roles, stands as a linchpin in the realms of neuroscience, embryogenesis, and disease. Its multifaceted contributions to neural development, tissue morphogenesis, and disease pathogenesis underscore its significance in both health and pathology. As researchers continue to unravel FLRT3’s complexities, they not only deepen our understanding of fundamental biological processes but also pave the way for groundbreaking discoveries in neuroscience and therapeutic interventions, ultimately shaping the future landscape of medicine and scientific inquiry.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Tyrosine Kinase ErbB-4 Human Recombinant

Receptor tyrosine-protein kinase erbB-4, Proto-oncogene-like protein c-ErbB-4, Tyrosine kinase-type cell surface receptor HER4, p180erbB4, 4ICD, E4ICD, s80HER4, ERBB4, HER4, receptor tyrosine-protein kinase erbB-4 isoform JM-a/CVT-1, receptor tyrosine-protein kinase erbB-4, tyrosine kinase-type cell surface receptor HER4, avian erythroblastic leukemia viral (v-erb-b2) oncogene homolog 4, proto-oncogene-like protein c-ErbB-4, ALS19, v-erb-a erythroblastic leukemia viral oncogene homolog 4, v-erb-b2 avian erythroblastic leukemia viral oncogene homolog 4, human epidermal growth factor receptor 4.

Product # :

PKA-128

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Description

ErbB4 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 863 amino acids (26-649 a.a) and having a molecular mass of 96.6 kDa.ErbB4 is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The ErbB4 solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured by its binding ability in a functional ELISA with Human NRG1(CAT# cyt-1186). The ED50 range ≤ 0.2 ug/ml.

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Introduction
Tyrosine Kinase ErbB-4 (ErbB4) is a receptor tyrosine kinase that is a member of the epidermal growth factor receptor family whose members play a role as receptors for the EGF family of growth factors. ErbB4is a single-pass type I transmembrane protein with multiple furin-like cysteine rich domains,PDZ domain binding motif, a tyrosine kinase domain and a phosphotidylinositol-3 kinase binding site. ErbB4binds its ligands with low affinity and is expressed in normal skeletal muscle, heart, pituitary, brain and some breast carcinomas. Monomeric ErbB4 takes part in neuronal development and development of the heart and cancer.
Synonyms
Receptor tyrosine-protein kinase erbB-4, Proto-oncogene-like protein c-ErbB-4, Tyrosine kinase-type cell surface receptor HER4, p180erbB4, 4ICD, E4ICD, s80HER4, ERBB4, HER4, receptor tyrosine-protein kinase erbB-4 isoform JM-a/CVT-1, receptor tyrosine-protein kinase erbB-4, tyrosine kinase-type cell surface receptor HER4, avian erythroblastic leukemia viral (v-erb-b2) oncogene homolog 4, proto-oncogene-like protein c-ErbB-4, ALS19, v-erb-a erythroblastic leukemia viral oncogene homolog 4, v-erb-b2 avian erythroblastic leukemia viral oncogene homolog 4, human epidermal growth factor receptor 4.
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
QSVCAGTENK LSSLSDLEQQ YRALRKYYEN CEVVMGNLEI TSIEHNRDLS FLRSVREVTG YVLVALNQFR YLPLENLRII RGTKLYEDRY ALAIFLNYRK DGNFGLQELG LKNLTEILNG GVYVDQNKFL CYADTIHWQD IVRNPWPSNL TLVSTNGSSG CGRCHKSCTG RCWGPTENHC QTLTRTVCAE QCDGRCYGPY VSDCCHRECA GGCSGPKDTD CFACMNFNDS GACVTQCPQT FVYNPTTFQL EHNFNAKYTY GAFCVKKCPH NFVVDSSSCV RACPSSKMEV EENGIKMCKP CTDICPKACD GIGTGSLMSA QTVDSSNIDK FINCTKINGN LIFLVTGIHG DPYNAIEAID PEKLNVFRTV REITGFLNIQ SWPPNMTDFS VFSNLVTIGG RVLYSGLSLL ILKQQGITSL QFQSLKEISA GNIYITDNSN LCYYHTINWT TLFSTINQRI VIRDNRKAEN CTAEGMVCNH LCSSDGCWGP GPDQCLSCRR FSRGRICIES CNLYDGEFRE FENGSICVEC DPQCEKMEDG LLTCHGPGPD NCTKCSHFKD GPNCVEKCPD GLQGANSFIF KYADPDRECH PCHPNCTQGC NGPTSHDCIY YPWTGHSTLP QHARLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH HHH

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Erythropoietin Receptor Human Recombinant, Active

EPO-R, EPOR, Erythropoietin Receptor.

Product # :

CYT-997

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Description

EPOR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 232 amino acids (25-250a.a.) and having a molecular mass of 25.6kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).EPOR is expressed with a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 95.0% as determined by analysis by SDS-PAGE.

Biological Activity

Measured by its ability to inhibit EPO dependent proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect less or equal to 70ng/ml.

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Introduction
Erythropoietin receptor, also known as EPOR arbitrates erythropoietin-induced erythroblast proliferation as well as differentiation. During EPO binding, EPOR activates Jak2 tyrosine kinase which activates various intracellular pathways including: Ras/MAP kinase, phosphatidylinositol 3-kinase and STAT transcription factors. Furthermore, stimulated EPOR has a function in erythroid cell survival. Mutations in EPOR may possibly produce erythroleukemia and familial erythrocytosis. In addition, dysregulation of EPOR can affect on the growth of selected tumors.
Synonyms
EPO-R, EPOR, Erythropoietin Receptor.
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
APPPNLPDPK FESKAALLAA RGPEELLCFT ERLEDLVCFW EEAASAGVGP GNYSFSYQLE DEPWKLCRLH QAPTARGAVR FWCSLPTADT SSFVPLELRV TAASGAPRYH RVIHINEVVL LDAPVGLVAR LADESGHVVL RWLPPPETPM TSHIRYEVDV SAGNGAGSVQ RVEILEGRTE CVLSNLRGRT RYTFAVRARM AEPSFGGFWS AWSEPVSLLT PSDLDPHHHH HH.
Background
What is the molecular weight/Mw of ERYTHROPOIETIN Protein?
ERYTHROPOIETIN Protein has a total Mw of 25.6kDa.

What is the source or expression system of ERYTHROPOIETIN Protein?
Sf9, Baculovirus cells.

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

What is the Biological Activity of ERYTHROPOIETIN Protein?
Measured by its ability to inhibit EPO dependent proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect less or equal to 70ng/ml.

What is the amino acid sequence of ERYTHROPOIETIN Protein?
APPPNLPDPK FESKAALLAA RGPEELLCFT ERLEDLVCFW EEAASAGVGP GNYSFSYQLE DEPWKLCRLH QAPTARGAVR FWCSLPTADT SSFVPLELRV TAASGAPRYH RVIHINEVVL LDAPVGLVAR LADESGHVVL RWLPPPETPM TSHIRYEVDV SAGNGAGSVQ RVEILEGRTE CVLSNLRGRT RYTFAVRARM AEPSFGGFWS AWSEPVSLLT PSDLDPHHHH HH.

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

What is the endotoxin level for ERYTHROPOIETIN Protein?
The endotoxin level is minimal, ERYTHROPOIETIN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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